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the other side of the fiber and some dispersed flakes are visible.”*’’ This confirms that, in light scorches on the main Shroud, there is a scorched strippable flaked coating that is similar to the one in the lightly scorched Raes corner. More arguments for the presence of a starch-madder coating on the whole Shroud have already been published in 2012.%° Now, this chapter will extend this evidence, and the next chapter will differentiate between madder and Saponaria, showing there is much evidence against the presence of Saponaria.

Figure 62 the other side of the fiber and some dispersed flakes are visible.”*’’ This confirms that, in light scorches on the main Shroud, there is a scorched strippable flaked coating that is similar to the one in the lightly scorched Raes corner. More arguments for the presence of a starch-madder coating on the whole Shroud have already been published in 2012.%° Now, this chapter will extend this evidence, and the next chapter will differentiate between madder and Saponaria, showing there is much evidence against the presence of Saponaria.

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Fig. 2.1. Blood in area of the soles of the feet, screenshot of Shroud Scope, Durante 20027° 2.1.1. Acid heme dimers
Fig. 2.1. Blood in area of the soles of the feet, screenshot of Shroud Scope, Durante 20027° 2.1.1. Acid heme dimers
Fig. 2.2. Absorbance spectra: A of “a brownish red stained fibril from one of the blood areas of t Shroud”; “B, transmission spectrum obtained by transformation of the reflection spectrum of t blood areas of the Shroud” ©OSA *!
Fig. 2.2. Absorbance spectra: A of “a brownish red stained fibril from one of the blood areas of t Shroud”; “B, transmission spectrum obtained by transformation of the reflection spectrum of t blood areas of the Shroud” ©OSA *!
” The investigated Shroud fibers are called “a single microfiber ... garnet red” (Heller, Report on 126), and “seven microfibers with red stains on part of their length” (Heller, Report on..., 1983, 128) and “brownish red” (Heller and Adler, Blood on the Shroud..., 1980, TOM 30 and its fig.2 on TOM 31) by Heller and Adler, who saw these samples through the microscope, probably in transmitted light. See their article pages (TOM 30-31) with a plot of one of the transmission spectra showing a strong absorption band at 450 nm in fig. 2.2 A or through this link:
” The investigated Shroud fibers are called “a single microfiber ... garnet red” (Heller, Report on 126), and “seven microfibers with red stains on part of their length” (Heller, Report on..., 1983, 128) and “brownish red” (Heller and Adler, Blood on the Shroud..., 1980, TOM 30 and its fig.2 on TOM 31) by Heller and Adler, who saw these samples through the microscope, probably in transmitted light. See their article pages (TOM 30-31) with a plot of one of the transmission spectra showing a strong absorption band at 450 nm in fig. 2.2 A or through this link:
even a dissociated/lost protein and a remaining heme) and it is reminiscent of ‘turbidity’ (applying to the aggregation state of the heme compounds in solution). Fig. 2.4. Absorbance of methemoglobin at pH 1 to 12 (mirrored image) ©the American Society Biochemistry and Molecular Biology”
even a dissociated/lost protein and a remaining heme) and it is reminiscent of ‘turbidity’ (applying to the aggregation state of the heme compounds in solution). Fig. 2.4. Absorbance of methemoglobin at pH 1 to 12 (mirrored image) ©the American Society Biochemistry and Molecular Biology”
Fig. 2.5. B: Absorbance spectra of a buffered 1:4 water/methanol solution of heme monomer at pH 5.536 (solid line) and pH 8.862 (dotted line), and D: of a buffered aqueous solution of heme (dimer + a small monomer fraction) at pH 6.029 (solid line) and pH 9.669 (dotted line) ©Springer SBIC”’
Fig. 2.5. B: Absorbance spectra of a buffered 1:4 water/methanol solution of heme monomer at pH 5.536 (solid line) and pH 8.862 (dotted line), and D: of a buffered aqueous solution of heme (dimer + a small monomer fraction) at pH 6.029 (solid line) and pH 9.669 (dotted line) ©Springer SBIC”’
Fig. 2.6. Extinction coefficients of various heme products, dependent on pH ©AvdH Soret extinction coefficient might be 2 or even 1 x 10° M' cm’; this pH-dependence of the extinction coefficient is represented in fig. 2.6, showing the values given in table 1 of Villiers et al., 2007. This means that the extinction coefficients — and thus also the absorbance and reflectance values — of the Soret band and the 500 nm band of acid heme dimers in solution could be very close to each other at a low pH (<5). When aggregated or precipitated, the difference could be even less. % Villiers et al., Speciation and structure..., 2007, http://link.springer.com/article/10.1007%2Fs00775-006-0170-1
Fig. 2.6. Extinction coefficients of various heme products, dependent on pH ©AvdH Soret extinction coefficient might be 2 or even 1 x 10° M' cm’; this pH-dependence of the extinction coefficient is represented in fig. 2.6, showing the values given in table 1 of Villiers et al., 2007. This means that the extinction coefficients — and thus also the absorbance and reflectance values — of the Soret band and the 500 nm band of acid heme dimers in solution could be very close to each other at a low pH (<5). When aggregated or precipitated, the difference could be even less. % Villiers et al., Speciation and structure..., 2007, http://link.springer.com/article/10.1007%2Fs00775-006-0170-1
Fig. 2.7. Integrated reflectance and (one) transmission curve for laboratory blood preparations, including Shroud blood reflectance values (Pellicori) ©QOSA”
Fig. 2.7. Integrated reflectance and (one) transmission curve for laboratory blood preparations, including Shroud blood reflectance values (Pellicori) ©QOSA”
Table 1. Reference data of hemichrome and Pellicori’s artificially aged blood smear on linen. Pellicori’s two spectra of a blood smear on linen look as the spectrum of either alkaline methemoglobin (methemoglobin that has its iron ion OH-ligated at a physiological pH 7.25 — 7.4) and/or of hemichrome (methemoglobin without external ligand but that has its iron ion ligated to the hemoglobin’s own deformed protein at both axial sides and therefore is less influenced by pH), for it shows a shallow Soret band at ca. 410 nm, an even shallower Q band (= combined a and £ bands) in the 530-580 nm range, and only a very weak shoulder at ca. 600 nm. Maricic et al., 1964, published a transmission spectrum of the Q-region of hemichrome and called this methemoglobin species parahaemoglobin when they discovered its second formation path via the oxygen-free drying and then oxidation of hemoglobin, beside the already known path of the drying of methemoglobin.” In a study for forensic purposes, a non-linear least squares fit of reflectance spectra to determine the fractions of hree different heme compounds present in a 7-days-old bloodstain, resulted in 49% hemichrome, 16% methemoglobin, and 35% oxyhemoglobin; further ageing made the hemichrome fraction increase at the expense of oxyhemoglobin.” Also because of this result, one may assume that the blood smear that had been artificially aged by Pellicori by baking it in air for 7.5 hours at 60°C”, would largely have lost the iron’s aqueous ligand and consisted predominantly of hemichrome. Hemichrome’s characteristic values are as follows (table 1.):
Table 1. Reference data of hemichrome and Pellicori’s artificially aged blood smear on linen. Pellicori’s two spectra of a blood smear on linen look as the spectrum of either alkaline methemoglobin (methemoglobin that has its iron ion OH-ligated at a physiological pH 7.25 — 7.4) and/or of hemichrome (methemoglobin without external ligand but that has its iron ion ligated to the hemoglobin’s own deformed protein at both axial sides and therefore is less influenced by pH), for it shows a shallow Soret band at ca. 410 nm, an even shallower Q band (= combined a and £ bands) in the 530-580 nm range, and only a very weak shoulder at ca. 600 nm. Maricic et al., 1964, published a transmission spectrum of the Q-region of hemichrome and called this methemoglobin species parahaemoglobin when they discovered its second formation path via the oxygen-free drying and then oxidation of hemoglobin, beside the already known path of the drying of methemoglobin.” In a study for forensic purposes, a non-linear least squares fit of reflectance spectra to determine the fractions of hree different heme compounds present in a 7-days-old bloodstain, resulted in 49% hemichrome, 16% methemoglobin, and 35% oxyhemoglobin; further ageing made the hemichrome fraction increase at the expense of oxyhemoglobin.” Also because of this result, one may assume that the blood smear that had been artificially aged by Pellicori by baking it in air for 7.5 hours at 60°C”, would largely have lost the iron’s aqueous ligand and consisted predominantly of hemichrome. Hemichrome’s characteristic values are as follows (table 1.):
In Pellicori’s plot the depth of this ‘hemichrome’ Soret dip beneath the 500 nm value — at 500 nm the peak between the Soret dip and the 534 nm Q dip is located — is only ca. 0.079 relative reflectance units; the depth of the 534 nm dip beneath the 500 nm peak is 0.009 relative reflectance units and it represents an ¢ increase of 0.75, viz. from 0.72 to 1.47 10° M'' cm"! (cf. fig. 2.8). A linear approximation in this last short ¢ range (in the green wavelengths region), is that the relative reflectance value drops 0.012 reflectance units per 1.0 € unit increase. If this linear approximation is extrapolated to other possible small ¢ increases, the depth of the dimer’s Soret dip beneath its 500 nm value (the value which corresponds to an estimated e599 of 0.6 ¢ units”) may be estimated, if its spectrum was in Pellicori’s figure (fig. 2.7. above). The acid dimer’s Soret dip would be only 0.036 relative reflectance units deep if at pH 6.0 with €goret = 3.6, and it would be even smaller if at pH<5 (table 2). When a linear approximation between 0.72 and 10.5 € units (viz. a dip:e ratio of 0.008) is applied, as appropriate for the blue (Soret) region where the greatest loss of contrast takes place, the estimated dimer’s Soret dip would be only about 0.024 relative reflectance units deen if at no 60 with ew ,=—2 4 and again even cmaller if at nu<<« (fo 9 Q)
In Pellicori’s plot the depth of this ‘hemichrome’ Soret dip beneath the 500 nm value — at 500 nm the peak between the Soret dip and the 534 nm Q dip is located — is only ca. 0.079 relative reflectance units; the depth of the 534 nm dip beneath the 500 nm peak is 0.009 relative reflectance units and it represents an ¢ increase of 0.75, viz. from 0.72 to 1.47 10° M'' cm"! (cf. fig. 2.8). A linear approximation in this last short ¢ range (in the green wavelengths region), is that the relative reflectance value drops 0.012 reflectance units per 1.0 € unit increase. If this linear approximation is extrapolated to other possible small ¢ increases, the depth of the dimer’s Soret dip beneath its 500 nm value (the value which corresponds to an estimated e599 of 0.6 ¢ units”) may be estimated, if its spectrum was in Pellicori’s figure (fig. 2.7. above). The acid dimer’s Soret dip would be only 0.036 relative reflectance units deep if at pH 6.0 with €goret = 3.6, and it would be even smaller if at pH<5 (table 2). When a linear approximation between 0.72 and 10.5 € units (viz. a dip:e ratio of 0.008) is applied, as appropriate for the blue (Soret) region where the greatest loss of contrast takes place, the estimated dimer’s Soret dip would be only about 0.024 relative reflectance units deen if at no 60 with ew ,=—2 4 and again even cmaller if at nu<<« (fo 9 Q)
Fig. 2.9. Comparison of estimated depths of Soret dip of acid heme dimer (at various extinction coefficients) and ‘variations’ ©AvdH
Fig. 2.9. Comparison of estimated depths of Soret dip of acid heme dimer (at various extinction coefficients) and ‘variations’ ©AvdH
Fig. 2.10 Natural madder lake swatches ©L.L. Bispo”’ Chromatography was used to identify alizarin and purpurin in a red 7-9" century AD Coptic textile, in which iron was the sole, and apparently stable, mordant of these madder dyestuffs.”° Just as aluminum (AI°") is a mordant of madder dye and forms red madder lake (used in the paint called Rose Madder), also iron (probably Fe°*) is a mordant and can form madder lakes (pigment particles) and thereby paints of red and pink colors.”* When mixed in a binder, in a diluted form, Rose Madder pigments constitute a pink paint, but in a concentrated form, they may constitute a dull magenta-red paint.”” McCrone called the “rose madder particles” he had seen on the Shroud “red particles””® (cf. fig. 2.10). Therefore, the presence of a reddish heme-hydroxyanthraquinone compound (a red madder lake) on the Shroud, formed when acid heme was adsorbed to the Shroud’s coating of acid madder dye on starch, might be hypothesized.
Fig. 2.10 Natural madder lake swatches ©L.L. Bispo”’ Chromatography was used to identify alizarin and purpurin in a red 7-9" century AD Coptic textile, in which iron was the sole, and apparently stable, mordant of these madder dyestuffs.”° Just as aluminum (AI°") is a mordant of madder dye and forms red madder lake (used in the paint called Rose Madder), also iron (probably Fe°*) is a mordant and can form madder lakes (pigment particles) and thereby paints of red and pink colors.”* When mixed in a binder, in a diluted form, Rose Madder pigments constitute a pink paint, but in a concentrated form, they may constitute a dull magenta-red paint.”” McCrone called the “rose madder particles” he had seen on the Shroud “red particles””® (cf. fig. 2.10). Therefore, the presence of a reddish heme-hydroxyanthraquinone compound (a red madder lake) on the Shroud, formed when acid heme was adsorbed to the Shroud’s coating of acid madder dye on starch, might be hypothesized.
i Se ————————— — _e _e As already shown, the extinction coefficient of an acid heme dimer’s 393 nm Soret band is 3,6 x 10° M' cm’! at pH 6.0, and perhaps only 1,0 x 10* M' cm’ at pH 4.5. Whether or not also a shoulder resulting from an acid heme dimer transmittance was visible near 393 nm, or as far as 340 nm, in the stained fibril’s curve, we don’t know, for, in the published article, the curve is only plotted from 410 to 750 nm, probably because measurement below 410 nm was impossible because of the poor measurement conditions (glass slide, sticky tape and fibril in the way), which might also have shifted the peaks.''? Anyway, there is no suggestion of a 630 nm band, so perhaps the red on the fiber was not (only) heme. Perhaps there was (also) a red madder lake (= a madder-mordant complex), as there is a peak at ca. 530 nm and a pink/red madder lake’s absorbance maximum is in the 520-530 nm range'~” (fig. 2.14). See also the effect of mordanting on alizarin on wool in fig. 2.11. '*| Used from C. Clementi, W. Nowik, A. Romani, F. Cibin, G. Favaro, A spectrometric and chromatographic approach to the study of ageing of madder (Rubia tinctorum L.) dyestuff on wool, Analytica Chimica Acta, Vol. 596 Issue 1, July 2007, pp. 46-54, DOI: 10.1016/j.aca.2007.05.036, http://www.sciencedirect.com/science/article/pii/S0003267007009464 (fig. 2 http://ars.els-cdn.com/content/image/1-s2.0-S0003267007009464-gr2.jpg ) © 2007 Elsevier, with permission from Elsevier ie ean 12 ‘ae saps eee aan
i Se ————————— — _e _e As already shown, the extinction coefficient of an acid heme dimer’s 393 nm Soret band is 3,6 x 10° M' cm’! at pH 6.0, and perhaps only 1,0 x 10* M' cm’ at pH 4.5. Whether or not also a shoulder resulting from an acid heme dimer transmittance was visible near 393 nm, or as far as 340 nm, in the stained fibril’s curve, we don’t know, for, in the published article, the curve is only plotted from 410 to 750 nm, probably because measurement below 410 nm was impossible because of the poor measurement conditions (glass slide, sticky tape and fibril in the way), which might also have shifted the peaks.''? Anyway, there is no suggestion of a 630 nm band, so perhaps the red on the fiber was not (only) heme. Perhaps there was (also) a red madder lake (= a madder-mordant complex), as there is a peak at ca. 530 nm and a pink/red madder lake’s absorbance maximum is in the 520-530 nm range'~” (fig. 2.14). See also the effect of mordanting on alizarin on wool in fig. 2.11. '*| Used from C. Clementi, W. Nowik, A. Romani, F. Cibin, G. Favaro, A spectrometric and chromatographic approach to the study of ageing of madder (Rubia tinctorum L.) dyestuff on wool, Analytica Chimica Acta, Vol. 596 Issue 1, July 2007, pp. 46-54, DOI: 10.1016/j.aca.2007.05.036, http://www.sciencedirect.com/science/article/pii/S0003267007009464 (fig. 2 http://ars.els-cdn.com/content/image/1-s2.0-S0003267007009464-gr2.jpg ) © 2007 Elsevier, with permission from Elsevier ie ean 12 ‘ae saps eee aan
Fig. 2.12. Measured relative reflectance of bloodstains and absolute reflectance of clear area and calculated absolute reflectance of bloodstains ©CAvdH
Fig. 2.12. Measured relative reflectance of bloodstains and absolute reflectance of clear area and calculated absolute reflectance of bloodstains ©CAvdH
Here, where the linen and madder dye of the background do not interfere, the ca. 525 nm band is dominantly present. As (red) aluminum*’-alizarin and -purpurin complexes in methanol/water solution at pH 3.7 have absorbance maxima at 500 and 531 nm, respectively,'° and mordanted alizarin on wool has an absorbance peak at ca. 525 nm (fig. 2.11), and the absorbance peak of pink madder lake on a 6" century AD Byzantine manuscript is located at ca. 525 nm and its other peak is at ca. 280 nm (fig. 2.14),'°’ and the K/S absorption spectra of various red Al(OH)3-madder lakes have a peak at 507 nm, with a shoulder at 540 nm, and a band at ca. 280 nm (fig. 2.16),'** the bloodstains’ 525 nm band and smaller 280 nm band may very well result from red madder lake: heme-madder lake formed by acid heme dimers — these dimers probably produce the 340-410 (Soret)
Here, where the linen and madder dye of the background do not interfere, the ca. 525 nm band is dominantly present. As (red) aluminum*’-alizarin and -purpurin complexes in methanol/water solution at pH 3.7 have absorbance maxima at 500 and 531 nm, respectively,'° and mordanted alizarin on wool has an absorbance peak at ca. 525 nm (fig. 2.11), and the absorbance peak of pink madder lake on a 6" century AD Byzantine manuscript is located at ca. 525 nm and its other peak is at ca. 280 nm (fig. 2.14),'°’ and the K/S absorption spectra of various red Al(OH)3-madder lakes have a peak at 507 nm, with a shoulder at 540 nm, and a band at ca. 280 nm (fig. 2.16),'** the bloodstains’ 525 nm band and smaller 280 nm band may very well result from red madder lake: heme-madder lake formed by acid heme dimers — these dimers probably produce the 340-410 (Soret)
band, a 500 nm band(Q B band, linked to and lifted by the 525 nm lake band), the 630 nm band (charge transfer) band, and perhaps the small 725 nm band as well. If the Shroud’s 500 nm heme band is indeed greatly lifted by a 525 nm madder lake band — even to the level of the heme’s Soret band -, the original heme without madder lake could have had a Soret band that was considerably higher than its 500 nm band. This means that the heme dimer needn’t have had an extremely small Soret extinction coefficient (less than 2,5-3, cf. fig. 2.9) to lose the contrast of its Soret band in relative reflectance, but it may have been near the value, which Villiers et al. measured for the aqueous heme dimers without (higher) aggregation at pH 6.0, viz. 3.6 10° M' cm’! (cf. fig. 2.6).
band, a 500 nm band(Q B band, linked to and lifted by the 525 nm lake band), the 630 nm band (charge transfer) band, and perhaps the small 725 nm band as well. If the Shroud’s 500 nm heme band is indeed greatly lifted by a 525 nm madder lake band — even to the level of the heme’s Soret band -, the original heme without madder lake could have had a Soret band that was considerably higher than its 500 nm band. This means that the heme dimer needn’t have had an extremely small Soret extinction coefficient (less than 2,5-3, cf. fig. 2.9) to lose the contrast of its Soret band in relative reflectance, but it may have been near the value, which Villiers et al. measured for the aqueous heme dimers without (higher) aggregation at pH 6.0, viz. 3.6 10° M' cm’! (cf. fig. 2.6).
'° Reprinted from Spectrochimica Acta Part A: Molecular and Biomolecular Spectroscopy, Vol 95, September 2012, M. Aceto, A. Agostino, G. Fenoglio, P. Baraldi, P. Zannini, C. Hofmann, E. Gamillscheg, First analytical evidences of precious colourants on Mediterranean illuminated manuscripts, Pages 235-245, Copyright 2012, with permission from Elsevier. (Fig. 7 of http://dx.doi.org/10.1016/j.saa.2012.04.103 = http://www.sciencedirect.com/science/article/pii/S 13861425 12004568) '° http://commons.wikimedia.org/wiki/File:Cheirongruppe (Wiener _Dioskurides).jpg
'° Reprinted from Spectrochimica Acta Part A: Molecular and Biomolecular Spectroscopy, Vol 95, September 2012, M. Aceto, A. Agostino, G. Fenoglio, P. Baraldi, P. Zannini, C. Hofmann, E. Gamillscheg, First analytical evidences of precious colourants on Mediterranean illuminated manuscripts, Pages 235-245, Copyright 2012, with permission from Elsevier. (Fig. 7 of http://dx.doi.org/10.1016/j.saa.2012.04.103 = http://www.sciencedirect.com/science/article/pii/S 13861425 12004568) '° http://commons.wikimedia.org/wiki/File:Cheirongruppe (Wiener _Dioskurides).jpg
Fig. 2.16 Absorbance spectra of red lakes in Kubelka-Munk (k/s) value; madder P = prepared from plant root extract, R and F = prepared from extract of dyed wool samples ©Springer Science+Business Media'*’
Fig. 2.16 Absorbance spectra of red lakes in Kubelka-Munk (k/s) value; madder P = prepared from plant root extract, R and F = prepared from extract of dyed wool samples ©Springer Science+Business Media'*’
Fig. 2.17. Possible composition of the PRO spectrum (based on k/s values) of Shroud bloodstains ©AvdH
Fig. 2.17. Possible composition of the PRO spectrum (based on k/s values) of Shroud bloodstains ©AvdH
Just as an illustration, see the visible color change, which accompanies the absorbance peak shift induced by the binding of boronic acid to alizarin red S'*, a synthetic, sulphonated form of alizarin'® in fig. 2.18.
Just as an illustration, see the visible color change, which accompanies the absorbance peak shift induced by the binding of boronic acid to alizarin red S'*, a synthetic, sulphonated form of alizarin'® in fig. 2.18.
(fig. 2.20) In the heme-madder lake hypothesis, all reddish bloodstained fiber parts must have a madder lake coating, and therefore must have had a madder dye coating before the blood got unto it; in other words, image formation did not remove the madder dye before the blood got unto it, so, there was and is no image under the reddish bloodstained fiber parts. If blood got unto an image area after image formation, the madder-coated non-image fibers in the image would have colored red, but the madderless image fibers in the area would have colored brown or black, determining the brownishness of the overall color of the bloodstain, proportional to the percentage of image fibers — the local image density — in the area. Nothing of such an image-density-dependent brown is seen in bloodstains. This means that all fibers that got blood on them probably were non-image fibers: the blood was present before the image was formed.
(fig. 2.20) In the heme-madder lake hypothesis, all reddish bloodstained fiber parts must have a madder lake coating, and therefore must have had a madder dye coating before the blood got unto it; in other words, image formation did not remove the madder dye before the blood got unto it, so, there was and is no image under the reddish bloodstained fiber parts. If blood got unto an image area after image formation, the madder-coated non-image fibers in the image would have colored red, but the madderless image fibers in the area would have colored brown or black, determining the brownishness of the overall color of the bloodstain, proportional to the percentage of image fibers — the local image density — in the area. Nothing of such an image-density-dependent brown is seen in bloodstains. This means that all fibers that got blood on them probably were non-image fibers: the blood was present before the image was formed.
Fig. 2.20. Relative reflectance spectra of four bloodstains ©OSA '*°
Fig. 2.20. Relative reflectance spectra of four bloodstains ©OSA '*°
=) Whadder lake b) Pink madder c) Purple madder (Hrassean, 2011, Fig. 58>
=) Whadder lake b) Pink madder c) Purple madder (Hrassean, 2011, Fig. 58>
online at http:// www.sindone.info/ADLER.PDF) . '© Adapted from A.D. Adler, R. Selzer, and F. DeBlase, Further Spectroscopic Investigations of Samples of the Shroud of Turin, The Shroud of Turin - Unraveling the Mystery - Proceedings of the 1998 Dallas Symposium, Compiled by Michael Minor, Alexander Books, Alexander — North Carolina, 2002, pp. 166-18, © A.D. Adler, R. Selzer, F. DeBlase, with permission from R. Selzer. '63 Brosseau et al., Revealing the invisible..., 2011, http:// sites. weinberg.northwestern. edu/ vanduyne/. files/2012/10/2011 Brosseau.pdf
online at http:// www.sindone.info/ADLER.PDF) . '© Adapted from A.D. Adler, R. Selzer, and F. DeBlase, Further Spectroscopic Investigations of Samples of the Shroud of Turin, The Shroud of Turin - Unraveling the Mystery - Proceedings of the 1998 Dallas Symposium, Compiled by Michael Minor, Alexander Books, Alexander — North Carolina, 2002, pp. 166-18, © A.D. Adler, R. Selzer, F. DeBlase, with permission from R. Selzer. '63 Brosseau et al., Revealing the invisible..., 2011, http:// sites. weinberg.northwestern. edu/ vanduyne/. files/2012/10/2011 Brosseau.pdf
As can be seen below in the FTIR plot of a simulated traumatic blood clot exudate (three drops of whole blood mixed with three drops of a bilirubin/albumin solution’®), called “simulated” in fig. 10 of Adler et al. 2002'% (fig. 2.25) and its wavenumber values (table 3), the blood globs’ FTIRs are a much closer match to the FTIRs of madder lake — even without adding the broad round heme band above 3000 cm’ — than to the FTIR of the simulacrum.
As can be seen below in the FTIR plot of a simulated traumatic blood clot exudate (three drops of whole blood mixed with three drops of a bilirubin/albumin solution’®), called “simulated” in fig. 10 of Adler et al. 2002'% (fig. 2.25) and its wavenumber values (table 3), the blood globs’ FTIRs are a much closer match to the FTIRs of madder lake — even without adding the broad round heme band above 3000 cm’ — than to the FTIR of the simulacrum.
Fig. 2.26 (left). Fluorescence emission spectra of mixtures of purpurin lakes and alizarin lakes (bottom to top curves: 0:100 , 20:80 40:60 , 60:40, 80:20 and 100:0 purpurin:alizarin) . 19] ©Elsevier excitation and a the two peaks a lake fluorescence. fluorimetry of bsorption minimum of both alizarin lake and pur ca. 300 and 500 nm'*’ (fig. 2.27). Excitation a 188 purin lake is at ca. 365 nm, between 440 nm still yields at least alizarin But the wavelengths of the excitation used in the fluorescence photography and he Turin Shroud in 1978 are 335-375 nm and 365 nm, respectively,'®’ and thus exactly in the excitation minimum for madder lake. A photo of the excitation-dependent fluorescence of madder lake madder fluorescence is visible. pigments in linseed oil (fig. 2.28) shows that und 190 er 365 nm excitation hardly any red
Fig. 2.26 (left). Fluorescence emission spectra of mixtures of purpurin lakes and alizarin lakes (bottom to top curves: 0:100 , 20:80 40:60 , 60:40, 80:20 and 100:0 purpurin:alizarin) . 19] ©Elsevier excitation and a the two peaks a lake fluorescence. fluorimetry of bsorption minimum of both alizarin lake and pur ca. 300 and 500 nm'*’ (fig. 2.27). Excitation a 188 purin lake is at ca. 365 nm, between 440 nm still yields at least alizarin But the wavelengths of the excitation used in the fluorescence photography and he Turin Shroud in 1978 are 335-375 nm and 365 nm, respectively,'®’ and thus exactly in the excitation minimum for madder lake. A photo of the excitation-dependent fluorescence of madder lake madder fluorescence is visible. pigments in linseed oil (fig. 2.28) shows that und 190 er 365 nm excitation hardly any red
Fig. 2.28. Appearance in white light and UV-fluorescence of various swatches of madder lake (Kremer Pigment) painted across non- fluorescing red ochre ©Antonino Cosentino, Culture Heritage Science Open Source, chsopensource.org sad
Fig. 2.28. Appearance in white light and UV-fluorescence of various swatches of madder lake (Kremer Pigment) painted across non- fluorescing red ochre ©Antonino Cosentino, Culture Heritage Science Open Source, chsopensource.org sad
Fig. 2.29. A part of the small of the back area of the Shroud in visible light (left) and UV light, showing fluorescence “slightly enhanced” (right) ©T. Heimburger'*”
Fig. 2.29. A part of the small of the back area of the Shroud in visible light (left) and UV light, showing fluorescence “slightly enhanced” (right) ©T. Heimburger'*”
Fig. 2.31. UV-fluorescence photo (cropped) oft thin and dense bloodflows in small of back area of the Shroud ©Biocommunications Association, Inc.'””
Fig. 2.31. UV-fluorescence photo (cropped) oft thin and dense bloodflows in small of back area of the Shroud ©Biocommunications Association, Inc.'””
Fig. 2.32. Smoothed fluorescence curves of four clear areas of the Shroud ©OSA™"! The ratio of the intensities of the fluorescence at 450 nm (F459, the datapoint with the highest intensity) and at 600 nm (Feoo, the datapoint closest to 620 nm, the fluorescence maximum of madder lake) can be calculated from the fluorescence spectra of background, image, bloodstains, and scorches, which were published in spectra showing datapoints at 50 nm intervals (the experimental set-up had a 17 nm-resolution) (e.g. fig. 2.32 and 2.33). The smaller the ratio, the redder the visible color of the total fluorescence. The values derived from the spectra published in the article of the Gilberts” are presented in table 4 and figure 2.34.
Fig. 2.32. Smoothed fluorescence curves of four clear areas of the Shroud ©OSA™"! The ratio of the intensities of the fluorescence at 450 nm (F459, the datapoint with the highest intensity) and at 600 nm (Feoo, the datapoint closest to 620 nm, the fluorescence maximum of madder lake) can be calculated from the fluorescence spectra of background, image, bloodstains, and scorches, which were published in spectra showing datapoints at 50 nm intervals (the experimental set-up had a 17 nm-resolution) (e.g. fig. 2.32 and 2.33). The smaller the ratio, the redder the visible color of the total fluorescence. The values derived from the spectra published in the article of the Gilberts” are presented in table 4 and figure 2.34.
Table 4. Fluorescence values of various areas of the Shroud, derived from Gilbert and Gilbert, 198 fig. 7, 11, 13, and 17 (F459 = fluorescence intensity at 450 nm, F609 = fluorescence intensity at 6¢ nm, in arbitrary units of a scale variable)
Table 4. Fluorescence values of various areas of the Shroud, derived from Gilbert and Gilbert, 198 fig. 7, 11, 13, and 17 (F459 = fluorescence intensity at 450 nm, F609 = fluorescence intensity at 6¢ nm, in arbitrary units of a scale variable)
Fig. 2.33. Smoothed fluorescence curves of three bloodstains of the Shroud ©OSA*”
Fig. 2.33. Smoothed fluorescence curves of three bloodstains of the Shroud ©OSA*”
They show that the mean F450/Feoo ratio of the bloodstains is smaller than that of the image and much smaller than that of the background. Of the image it is said that “as the fluorescen ce level is reduced, the peak shifts slightly to longer wavelengths” and “these stains [image and scorch] seem to exhibit a low level fluorescence of their own in the 600-700 nm region. This lower level fluorescence is » 203 somewhat more pronounced with the scorched areas than the body image areas”.~”” Looking at the mean F450/Feo0 values above, it can certainly be said that the bloodstains, althoug fluorescence, also seem to have a low level fluorescence of their own in the 600-700 nm region, even in more pronounced way than the image areas. Although Gilbert and Gilbert say about t bloodstains that “There is little evidence of shifting of the peak fluorescence to longer hat there is a red fluorescence contribution that pulls t 99204 wavelengths” ’, this doesn brown heme deposits (absor fluorescence of madde lake presence of weakly red fluoresceing mad han the fluorescence of dense bloodstains (cf. fig. 2.31 *t preclude balance to the red. This red shift, that may also be partly due bing more in the blue and green t has more reddening power than t background fluorescence red , but just a bit weaker. to the fluorescence quenching effect han in the red), might also be due to t der lake. The fluorescence of faint bloodstains looks redd ), perhaps because the intrinsic red he absorbance of heme deposits. A very hin heme deposit alone probably would not have turned the relatively strong green yellow h weaker in overall ne he of he er
They show that the mean F450/Feoo ratio of the bloodstains is smaller than that of the image and much smaller than that of the background. Of the image it is said that “as the fluorescen ce level is reduced, the peak shifts slightly to longer wavelengths” and “these stains [image and scorch] seem to exhibit a low level fluorescence of their own in the 600-700 nm region. This lower level fluorescence is » 203 somewhat more pronounced with the scorched areas than the body image areas”.~”” Looking at the mean F450/Feo0 values above, it can certainly be said that the bloodstains, althoug fluorescence, also seem to have a low level fluorescence of their own in the 600-700 nm region, even in more pronounced way than the image areas. Although Gilbert and Gilbert say about t bloodstains that “There is little evidence of shifting of the peak fluorescence to longer hat there is a red fluorescence contribution that pulls t 99204 wavelengths” ’, this doesn brown heme deposits (absor fluorescence of madde lake presence of weakly red fluoresceing mad han the fluorescence of dense bloodstains (cf. fig. 2.31 *t preclude balance to the red. This red shift, that may also be partly due bing more in the blue and green t has more reddening power than t background fluorescence red , but just a bit weaker. to the fluorescence quenching effect han in the red), might also be due to t der lake. The fluorescence of faint bloodstains looks redd ), perhaps because the intrinsic red he absorbance of heme deposits. A very hin heme deposit alone probably would not have turned the relatively strong green yellow h weaker in overall ne he of he er
Figure 1. Evolution of the absorption spectrum of 1,2-HAQ (3.0 x 10-° mol dm~?) in water—dioxane solutions (2:1, v/v) as a function of pH. Light grey, pH =2 (neutral form); grey, pH = 9 (mono-anion); black, pH = 14 (di-anion). Arrows indicate isosbestic points between the neutral form and mono-anion (a, 463 nm) and between the mono-anion and di-anion (b, 516 nm)
Figure 1. Evolution of the absorption spectrum of 1,2-HAQ (3.0 x 10-° mol dm~?) in water—dioxane solutions (2:1, v/v) as a function of pH. Light grey, pH =2 (neutral form); grey, pH = 9 (mono-anion); black, pH = 14 (di-anion). Arrows indicate isosbestic points between the neutral form and mono-anion (a, 463 nm) and between the mono-anion and di-anion (b, 516 nm)
Figure 2. Absorption (dotted line) and fluorescence (full line) normalized spectra of the three species derived from 1,2-HAQ in water—-dioxane solutions (2:1, v/v). Light grey, pH=2 (neutral form); grey, pH = 9 (mono-anion); black, pH = 14 (di-anion)
Figure 2. Absorption (dotted line) and fluorescence (full line) normalized spectra of the three species derived from 1,2-HAQ in water—-dioxane solutions (2:1, v/v). Light grey, pH=2 (neutral form); grey, pH = 9 (mono-anion); black, pH = 14 (di-anion)
Figure 4. Emission changes of 1,2,4-HAQ (2.3 x 107° mol dm~3) in water—dioxane (2:1 v/v) solutions as a function of pH; Aexc = 377 nm.). Light grey, pH = 2 (neutral form); grey, pH = 7 (mono-anion); black, pH = 14 (di-anion)
Figure 4. Emission changes of 1,2,4-HAQ (2.3 x 107° mol dm~3) in water—dioxane (2:1 v/v) solutions as a function of pH; Aexc = 377 nm.). Light grey, pH = 2 (neutral form); grey, pH = 7 (mono-anion); black, pH = 14 (di-anion)
Figure 3. Evolution of the absorption spectrum of 1,2,4-HAQ (3.3 x 10°? mol dm~?) in water-dioxane solutions (2:1, v/v) as a function of pH. Light grey, pH = 2 (neutral form); grey, pH =7 (mono-anion); black, pH = 14 (di- anion). Arrows indicate isosbestic points between the neutral form and mono- anion (a, 480 nm) and between the mono-anion and di-anion (b, 528 nm)
Figure 3. Evolution of the absorption spectrum of 1,2,4-HAQ (3.3 x 10°? mol dm~?) in water-dioxane solutions (2:1, v/v) as a function of pH. Light grey, pH = 2 (neutral form); grey, pH =7 (mono-anion); black, pH = 14 (di- anion). Arrows indicate isosbestic points between the neutral form and mono- anion (a, 480 nm) and between the mono-anion and di-anion (b, 528 nm)
Figure 5. Absorption (dotted line) and fluorescence (full line) normalized spectra of the three species of 1,2,4-HAQ in water— dioxane solutions (2:1, v/v). Light grey, pH = 2 (neutral form); grey, pH = 7 (mono-anion); black pH = 14 (di-anion) 2.1.2.5. Ehrlich’s reagent detected (madder) phenols in blood samples
Figure 5. Absorption (dotted line) and fluorescence (full line) normalized spectra of the three species of 1,2,4-HAQ in water— dioxane solutions (2:1, v/v). Light grey, pH = 2 (neutral form); grey, pH = 7 (mono-anion); black pH = 14 (di-anion) 2.1.2.5. Ehrlich’s reagent detected (madder) phenols in blood samples
“Table 6. Comparison of FTIR wavenumbers (cm") of free human serum albumin (HSA) and Shroud “serum” fibers (numbers estimated from plots and published numbers)”**
“Table 6. Comparison of FTIR wavenumbers (cm") of free human serum albumin (HSA) and Shroud “serum” fibers (numbers estimated from plots and published numbers)”**
Fig. 2.40. A: FTIR spectra of Shroud “serum fibers” ©A.D. Adler, R. Selzer, F. DeBlase”®” B: Comparison of FTIR spectra of Shroud “serum fibers” ©A.D. Adler, R. Selzer, F. DeBlase’”’, and FTIR spectra of Human Serum Albumin (blue = HSA in aqueous solution, red = dried HSA microcapsules) (mirrored figure) ©Elsevier’”!
Fig. 2.40. A: FTIR spectra of Shroud “serum fibers” ©A.D. Adler, R. Selzer, F. DeBlase”®” B: Comparison of FTIR spectra of Shroud “serum fibers” ©A.D. Adler, R. Selzer, F. DeBlase’”’, and FTIR spectra of Human Serum Albumin (blue = HSA in aqueous solution, red = dried HSA microcapsules) (mirrored figure) ©Elsevier’”!
“” Adapted from A.D. Adler, R. Selzer, and F. DeBlase, Further Spectroscopic Investigations of Samples of the Shroud of Turin, The Shroud of Turin - Unraveling the Mystery - Proceedings of the 1998 Dallas Symposium, Compiled by Michael Minor, Alexander Books, Alexander — North Carolina, 2002, pp. 166-181. (= fig. 8 on TOM 100), © A.D. Adler, R. Selzer, F. DeBlase, with permission from R. Selzer. ol HSA spectrum adapted (mirrored plot) from Gang Lu, Zhihua An, Junbai Li, Biogenic capsules made of proteins and
“” Adapted from A.D. Adler, R. Selzer, and F. DeBlase, Further Spectroscopic Investigations of Samples of the Shroud of Turin, The Shroud of Turin - Unraveling the Mystery - Proceedings of the 1998 Dallas Symposium, Compiled by Michael Minor, Alexander Books, Alexander — North Carolina, 2002, pp. 166-181. (= fig. 8 on TOM 100), © A.D. Adler, R. Selzer, F. DeBlase, with permission from R. Selzer. ol HSA spectrum adapted (mirrored plot) from Gang Lu, Zhihua An, Junbai Li, Biogenic capsules made of proteins and
Fig. 2.44. Detail from the negative of an ordinary white light photo of the dorsal legs and ankle: ©Shroud Scope, Durante 2002; white light photo, but all colors inverted and contrast-enhanced*”’
Fig. 2.44. Detail from the negative of an ordinary white light photo of the dorsal legs and ankle: ©Shroud Scope, Durante 2002; white light photo, but all colors inverted and contrast-enhanced*”’
Fig. 2.45. A: Serum draining from a blood clot on a glass plate that was placed from horizontal tc vertical 30 min after the fresh whole blood was dripped unto it and left to clot in a room at 18-19 °C 60-70% relative humidity. B: Sketch of hypothesized vertical serum draining and hemolysis and lake formation on the Shroud. ©AvdH
Fig. 2.45. A: Serum draining from a blood clot on a glass plate that was placed from horizontal tc vertical 30 min after the fresh whole blood was dripped unto it and left to clot in a room at 18-19 °C 60-70% relative humidity. B: Sketch of hypothesized vertical serum draining and hemolysis and lake formation on the Shroud. ©AvdH
An experiment showed that a glob of three drops of fresh whole blood from a finger stick, fallen on a glass plate straight from the finger, in a relatively cold environment (18-24 °C), clots in such a way that when a piece of linen is dropped on it from 1 cm above it, about an hour and a half after the release of the blood, a serum halo is formed in the cloth (fig. 2.46). Also when a similar bloodclot on a horizontal glass plate is placed vertical, half an hour after blood release, and a piece of linen is taped on it about an hour later, it is still possible to obtain a serum halo around the imprint on the cloth (fig. 2.47). *°8 T avoie et al., Blood on the Shroud... Part II, p UV photo is online in Fanti and Faccini, Sindone: 6 33° Weaver, Science seeks to solve..., 1980. Also in Ad a scienza spiega la fede, p. 11 http://www.dii.unipd.it/- er, Chemical and Physical..., 2000, fig. 2. TOM p. 14, and the giulio.fanti/research/Sindone/Mostra%20Sindone.pdf ; Although the resolution of this UV photo is not high, it seems th fluorescence results from a clearer margin in visib e lig ht (cf. http://www.dshroud.com/shroudScope/shroudScope.shtml?zl=10&image=3 &lon=3410&lat=14378) either from clear (diluted?) serum or perhaps from (orange) concen rated serum that largely abraded here after the UV photo was taken, leaving a light margin surrounded by the darker image of the side. *° Tackson, New Evidence that the Turin Shroud was t https:/Awww. youtube.com/watch?v=WGCi-FALo he Mandylion, presentation Rome 1993, Dg from 32:22; cf. Miller and Pellicori, Ultraviolet..., 1981, fig. 8
An experiment showed that a glob of three drops of fresh whole blood from a finger stick, fallen on a glass plate straight from the finger, in a relatively cold environment (18-24 °C), clots in such a way that when a piece of linen is dropped on it from 1 cm above it, about an hour and a half after the release of the blood, a serum halo is formed in the cloth (fig. 2.46). Also when a similar bloodclot on a horizontal glass plate is placed vertical, half an hour after blood release, and a piece of linen is taped on it about an hour later, it is still possible to obtain a serum halo around the imprint on the cloth (fig. 2.47). *°8 T avoie et al., Blood on the Shroud... Part II, p UV photo is online in Fanti and Faccini, Sindone: 6 33° Weaver, Science seeks to solve..., 1980. Also in Ad a scienza spiega la fede, p. 11 http://www.dii.unipd.it/- er, Chemical and Physical..., 2000, fig. 2. TOM p. 14, and the giulio.fanti/research/Sindone/Mostra%20Sindone.pdf ; Although the resolution of this UV photo is not high, it seems th fluorescence results from a clearer margin in visib e lig ht (cf. http://www.dshroud.com/shroudScope/shroudScope.shtml?zl=10&image=3 &lon=3410&lat=14378) either from clear (diluted?) serum or perhaps from (orange) concen rated serum that largely abraded here after the UV photo was taken, leaving a light margin surrounded by the darker image of the side. *° Tackson, New Evidence that the Turin Shroud was t https:/Awww. youtube.com/watch?v=WGCi-FALo he Mandylion, presentation Rome 1993, Dg from 32:22; cf. Miller and Pellicori, Ultraviolet..., 1981, fig. 8
15 days old, contact side, most crusts just removed
15 days old, contact side, most crusts just removed
28 days old, contact side
28 days old, contact side
Fig. 2.47. Vertical clot imprints on pure and starched-and-madder-dyed linen. Photos: 1.5 hour-old blood clots (placed vertical 30 min after blood was released from finger on horizontal glass plate in a room at 18-19 °C and 60-70% rel. humidity) right before imprinting; non-contact side, contact side seen through the reverse side of the glass plate, and contact side just lifted up from the blood clot, respectively, 24 hours after blood release. The red/orange flow away from the clot was caused by the manual turning around of the glass plate to see the reverse. Last photos: contact side, 15 days and 28 days after imprinting, and UV-fluorescence photo (Hoya L-42 UV filter, no blue-light filter), most loose crusts removed from the stain. ©CAvdH
Fig. 2.47. Vertical clot imprints on pure and starched-and-madder-dyed linen. Photos: 1.5 hour-old blood clots (placed vertical 30 min after blood was released from finger on horizontal glass plate in a room at 18-19 °C and 60-70% rel. humidity) right before imprinting; non-contact side, contact side seen through the reverse side of the glass plate, and contact side just lifted up from the blood clot, respectively, 24 hours after blood release. The red/orange flow away from the clot was caused by the manual turning around of the glass plate to see the reverse. Last photos: contact side, 15 days and 28 days after imprinting, and UV-fluorescence photo (Hoya L-42 UV filter, no blue-light filter), most loose crusts removed from the stain. ©CAvdH
Fig. 2.48. Fresh whole blood separating into serum and red material in a narrow plastic container, right after blood drawal, 1.5 hour after, and 16 hours after, respectively. CAvdH
Fig. 2.48. Fresh whole blood separating into serum and red material in a narrow plastic container, right after blood drawal, 1.5 hour after, and 16 hours after, respectively. CAvdH
Fig. 2.49. Fibers from sticky-tape 6AF, taken from the “lance wound” area of the Shroud, ventral image” ©2005 Raymond N. Rogers Collection, STERA, Inc.*””
Fig. 2.49. Fibers from sticky-tape 6AF, taken from the “lance wound” area of the Shroud, ventral image” ©2005 Raymond N. Rogers Collection, STERA, Inc.*””
concentrate containing saponins and with a foam number <100 had a non-zero hemolytic activity. viz. 1-2.°”° Still, it would be useful to know the exact species of the saponin(s) in Rubia tinctorum root. As the Lieberman-Burchard test is a test for cholesterol, which is a sterol,>”° madder root saponins probably include a sterol-type saponin, which is the type of saponin that generally gives much higher rates of hemolysis than the triterpene type.°”’ On the other hand, the bark (the outermost layer on stems and roots) of plants of the Rosaceae family, to which madder belongs, contains “very polar saponins” which are also present in Saponaria officinialis (the traditional soapwort) and which are “among the biggest with nine to ten oses bound to a pentacyclic triterpenoid acid” and are “hemolytic”.*”* tension, haemolytic activity, and toxicity after subcutaneous administration of saponin have been reported by Vacek anc Sedlak (1962).” http://www.sciencedirect.com/science/article/pii/0308814694901201 *”° “Hemolytic activity (hemolysis degree) 1-2 Foam indexa <100” , Escudero et al., 2004, Comparison of the chemical composition and nutritional value of Amaranthus cruentus flour and its protein concentrate, http://link.springer.com/article/10.1007/s11130-004-0033-3 376 http://en. wikipedia. org/wiki/Liebermann%E2%80%93Burchard_ test ; http://en.wikipedia.org/wiki/Cholesterol 377 “The name “saponin! denotes a large and chemically heterogeneous group of sterol glycosides and triterpene a rr ee, eS eae ee | ee © oe
concentrate containing saponins and with a foam number <100 had a non-zero hemolytic activity. viz. 1-2.°”° Still, it would be useful to know the exact species of the saponin(s) in Rubia tinctorum root. As the Lieberman-Burchard test is a test for cholesterol, which is a sterol,>”° madder root saponins probably include a sterol-type saponin, which is the type of saponin that generally gives much higher rates of hemolysis than the triterpene type.°”’ On the other hand, the bark (the outermost layer on stems and roots) of plants of the Rosaceae family, to which madder belongs, contains “very polar saponins” which are also present in Saponaria officinialis (the traditional soapwort) and which are “among the biggest with nine to ten oses bound to a pentacyclic triterpenoid acid” and are “hemolytic”.*”* tension, haemolytic activity, and toxicity after subcutaneous administration of saponin have been reported by Vacek anc Sedlak (1962).” http://www.sciencedirect.com/science/article/pii/0308814694901201 *”° “Hemolytic activity (hemolysis degree) 1-2 Foam indexa <100” , Escudero et al., 2004, Comparison of the chemical composition and nutritional value of Amaranthus cruentus flour and its protein concentrate, http://link.springer.com/article/10.1007/s11130-004-0033-3 376 http://en. wikipedia. org/wiki/Liebermann%E2%80%93Burchard_ test ; http://en.wikipedia.org/wiki/Cholesterol 377 “The name “saponin! denotes a large and chemically heterogeneous group of sterol glycosides and triterpene a rr ee, eS eae ee | ee © oe
Fig. 2.51. A and B: same extract, made by gently stirring Rubia tinctorum root powder in hot water for 45 min, spontaneously fermented in a closed glass jar. Photos two hours and four days after extraction, respectively. The pH dropped from 6.5-7 to 4.5-5, in these four days. C: a madder root ‘tea’ fermenting two days after preparation. CAvdH dye and fabric brightener on the fabric that would become the Shroud. Madder dye can even bs extracted from chopped and crushed madder root in cold water and also applied to fabric in colc water (room temperature) — this is the time-consuming ‘Nest Rubio’ technique for madder.**”’
Fig. 2.51. A and B: same extract, made by gently stirring Rubia tinctorum root powder in hot water for 45 min, spontaneously fermented in a closed glass jar. Photos two hours and four days after extraction, respectively. The pH dropped from 6.5-7 to 4.5-5, in these four days. C: a madder root ‘tea’ fermenting two days after preparation. CAvdH dye and fabric brightener on the fabric that would become the Shroud. Madder dye can even bs extracted from chopped and crushed madder root in cold water and also applied to fabric in colc water (room temperature) — this is the time-consuming ‘Nest Rubio’ technique for madder.**”’
area) at the water stain at the lower right corner of the photo; small rhombic ‘owls eyes’ in the upper and lower right of the at p. 78 (dorsal shoulders area), the photo are darker and blue in UV, but lighter than their surroundings in visible light; also at p. 80 (dorsal top of head area), the inside of the small stain, at the center of the lower margin of the photo, is more blue and darker than the stain’s surroundings in UV, but lighter in visible light; at p. 81 (ventra at the centre of the photo, on top and below, are more blue and shoulders area), parts of the ‘pears’, darker; at p. 83 (ventral below-knees area), both in the upper and lower part of the photo, the pear ha but lighter in visible light (see e.g. fig. 4.2). ves are more blue and darker in UV,
area) at the water stain at the lower right corner of the photo; small rhombic ‘owls eyes’ in the upper and lower right of the at p. 78 (dorsal shoulders area), the photo are darker and blue in UV, but lighter than their surroundings in visible light; also at p. 80 (dorsal top of head area), the inside of the small stain, at the center of the lower margin of the photo, is more blue and darker than the stain’s surroundings in UV, but lighter in visible light; at p. 81 (ventra at the centre of the photo, on top and below, are more blue and shoulders area), parts of the ‘pears’, darker; at p. 83 (ventral below-knees area), both in the upper and lower part of the photo, the pear ha but lighter in visible light (see e.g. fig. 4.2). ves are more blue and darker in UV,
Fig. 4.3. FTIR spectra of brown crust and thread region 2, Villarreal’s 2008 presentation ©R. Breault, Shroud of Turin Education Project Inc.” (green curve = crust; blue curve = shroud — region 2; The slide of Villarrael was projected and/or filmed in perspective, which made the horizontal scale slightly non-linear: toward lower wavenumbers (toward the right part of plot) the FTIR plot is slightly compressed. The vertical axes on the left and right are not parallel. For this figure, the screen shot of the video has been slightly rotated to render the right part of the plot strictly vertical; the left part of the plot is still skew.) These two FTIR spectra of Villarreal, most interestingly, are also very similar to the FTIR spectra of non-image fibers from the surface of the main Shroud, as published by Adler, Selzer, and DeBlase>”® (four FTIR spectra of non-image fibers, see fig. 4.4), and by Adler, in another article, in The Orphaned Manuscript on page 83 (one spectrum of a non-image fiber sample, in one plot with one spectrum of a “radiocarbon warp” fiber, and four other spectra, all represented in his figure 1, with a single and linear horizontal scale, see fig. 4.5).
Fig. 4.3. FTIR spectra of brown crust and thread region 2, Villarreal’s 2008 presentation ©R. Breault, Shroud of Turin Education Project Inc.” (green curve = crust; blue curve = shroud — region 2; The slide of Villarrael was projected and/or filmed in perspective, which made the horizontal scale slightly non-linear: toward lower wavenumbers (toward the right part of plot) the FTIR plot is slightly compressed. The vertical axes on the left and right are not parallel. For this figure, the screen shot of the video has been slightly rotated to render the right part of the plot strictly vertical; the left part of the plot is still skew.) These two FTIR spectra of Villarreal, most interestingly, are also very similar to the FTIR spectra of non-image fibers from the surface of the main Shroud, as published by Adler, Selzer, and DeBlase>”® (four FTIR spectra of non-image fibers, see fig. 4.4), and by Adler, in another article, in The Orphaned Manuscript on page 83 (one spectrum of a non-image fiber sample, in one plot with one spectrum of a “radiocarbon warp” fiber, and four other spectra, all represented in his figure 1, with a single and linear horizontal scale, see fig. 4.5).
Fig. 4.5. A: FTIR spectra of Adler’s figure I of “Updating Recent Studies on the Shroud of Turin 1996 (The Orphaned Manuscript p. 83), ©ACS *'° B: Idem, covered with lath ©CACS *'”
Fig. 4.5. A: FTIR spectra of Adler’s figure I of “Updating Recent Studies on the Shroud of Turin 1996 (The Orphaned Manuscript p. 83), ©ACS *'° B: Idem, covered with lath ©CACS *'”
4.1.3.3. Linen, cotton and starch FTIRs are similar to each other and to Shroud FTIRs In fact, the FTIR spectra of linen, cotton and starch are very similar to each other (see fig. 4 below), which is only natural, as these materials all mainly consist of glucose units, either linked each other by beta linkage in cellulose (in linen and cotton) or by alpha linkage in starch. In 2011, was said and shown: “In FTIR analysis (Fig. 4), since the chemical nature of starch and cellulose mostly similar, many of the characteristic peaks overlap and hence distinction is difficult.”°*! Th means that the cotton fiber percentages, found in Raes and radiocarbon threads by Rogers (10-20! long cotton fibers in thread R7, also in the core of this cotton-linen blend thread) and by Fanti (2' thin cotton contamination, in a linen thread from just next to the radiocarbon sample), are n contradicted by FTIR results, and that these results also do not readily preclude or show the presen of the starch that was detected on Raes threads and fibers by wet chemistry.>*
4.1.3.3. Linen, cotton and starch FTIRs are similar to each other and to Shroud FTIRs In fact, the FTIR spectra of linen, cotton and starch are very similar to each other (see fig. 4 below), which is only natural, as these materials all mainly consist of glucose units, either linked each other by beta linkage in cellulose (in linen and cotton) or by alpha linkage in starch. In 2011, was said and shown: “In FTIR analysis (Fig. 4), since the chemical nature of starch and cellulose mostly similar, many of the characteristic peaks overlap and hence distinction is difficult.”°*! Th means that the cotton fiber percentages, found in Raes and radiocarbon threads by Rogers (10-20! long cotton fibers in thread R7, also in the core of this cotton-linen blend thread) and by Fanti (2' thin cotton contamination, in a linen thread from just next to the radiocarbon sample), are n contradicted by FTIR results, and that these results also do not readily preclude or show the presen of the starch that was detected on Raes threads and fibers by wet chemistry.>*
For comparison, see the FTIR spectrum of Gum Arabic (fig. 4.10). Here the relative intensities of the three low-wavenumber bands are unlike those of the Raes thread or even Raes crust. Because no protein has been found in the Raes corner, the presence of Gum Arabic — which does contain proteins —has already been precluded anyway.” Also, the cotton fibers found in the Raes corner were spun-
For comparison, see the FTIR spectrum of Gum Arabic (fig. 4.10). Here the relative intensities of the three low-wavenumber bands are unlike those of the Raes thread or even Raes crust. Because no protein has been found in the Raes corner, the presence of Gum Arabic — which does contain proteins —has already been precluded anyway.” Also, the cotton fibers found in the Raes corner were spun-
Fig. 4.12. FTIR spectra (detail 1500-1800 cm”, in transmission mode) of a folded cloth of white linen, heated in an closed container, as presented by Moroni, in Rome 1993.°** A (red): yellowed fibers (“image”) yield a clear 1640 cm’ peak; B (blue curve): white fibers (“background”) yield 1720, 1656, 1505 and 1562 cm” peaks. ©R. Breault’”
Fig. 4.12. FTIR spectra (detail 1500-1800 cm”, in transmission mode) of a folded cloth of white linen, heated in an closed container, as presented by Moroni, in Rome 1993.°** A (red): yellowed fibers (“image”) yield a clear 1640 cm’ peak; B (blue curve): white fibers (“background”) yield 1720, 1656, 1505 and 1562 cm” peaks. ©R. Breault’”
Table 7. FTIR wavenumbers of various relevant substances. Dark green: cotton®”’; light green: linen’; dar blue: starches”! (light blue marking the a-link wavenumbers); light blue: amylopectin’™; light orange: alizarin’®; dar orange: purpurin’™; brown: squalene’; white: Shroud samples (1“ boxed-in column Raes crust thin; then one colum Raes crust bulk, three columns Raes thread #1, one column Reas thread #7, one column Raes thread #14", four columr radiocarbon area weft, four columns radiocarbon area inner warp, five boxed-in columns non-image, three columr image, two columns backing cloth (light blue and yellow marking starch and madder wavenumbers, respectively’”’).
Table 7. FTIR wavenumbers of various relevant substances. Dark green: cotton®”’; light green: linen’; dar blue: starches”! (light blue marking the a-link wavenumbers); light blue: amylopectin’™; light orange: alizarin’®; dar orange: purpurin’™; brown: squalene’; white: Shroud samples (1“ boxed-in column Raes crust thin; then one colum Raes crust bulk, three columns Raes thread #1, one column Reas thread #7, one column Raes thread #14", four columr radiocarbon area weft, four columns radiocarbon area inner warp, five boxed-in columns non-image, three columr image, two columns backing cloth (light blue and yellow marking starch and madder wavenumbers, respectively’”’).
Fig. 4.15. FTIR spectrum of purpurin, Photograph ©2013 Museum of Fine Arts, Boston’™ Missing peaks Villarreal’s slide introducing the FTIR analysis read: “Analysis was performed using an FTIR microscope in reflectance mode, sampling at most a few fibers per spectrum. Several (4-6) spectra were obtained at each chosen position along the length of the thread. Issue: Some spectral characteristics depend on the vertical position of the fibers relative to the focal plane (fibers must lie flat for reliable data).”°”° So, if some linen, starch or madder peaks are missing in some Raes FTIRs, this may be one of the reasons. The FTIRs by Adler, Selzer and DeBlase were measured in transmission mode. Other reasons for the missing of some madder peaks may be: 1) madder would have been largely washed off by the xylene/toluene that washed off the sticky-tape adhesive (see 4.2.1.1.), 2) madder peaks were dominated by the much larger presence of linen, and probably even of starch, and 3) madder consists of more than just alizarin and purpurin, and therefore madder peaks may be a bit shifted from the locations of peaks of pure undegraded alizarin and purpurin.
Fig. 4.15. FTIR spectrum of purpurin, Photograph ©2013 Museum of Fine Arts, Boston’™ Missing peaks Villarreal’s slide introducing the FTIR analysis read: “Analysis was performed using an FTIR microscope in reflectance mode, sampling at most a few fibers per spectrum. Several (4-6) spectra were obtained at each chosen position along the length of the thread. Issue: Some spectral characteristics depend on the vertical position of the fibers relative to the focal plane (fibers must lie flat for reliable data).”°”° So, if some linen, starch or madder peaks are missing in some Raes FTIRs, this may be one of the reasons. The FTIRs by Adler, Selzer and DeBlase were measured in transmission mode. Other reasons for the missing of some madder peaks may be: 1) madder would have been largely washed off by the xylene/toluene that washed off the sticky-tape adhesive (see 4.2.1.1.), 2) madder peaks were dominated by the much larger presence of linen, and probably even of starch, and 3) madder consists of more than just alizarin and purpurin, and therefore madder peaks may be a bit shifted from the locations of peaks of pure undegraded alizarin and purpurin.
Fig. 4.16. F TIR of “What appeared to be a thin fragment of crust”, green curve = “crust”, black curve = “linen standard”, 2008 presentation of Villarreal ©R. Breault, Shroud of Turin Education Project Inc. all the large piece of crust “may be dominated by embedded fibers”.°” Also, all large peaks of the Raes/radiocarbon and main Shroud non-image FTIRs can be assigned to linen, starch and alizarin/purpurin. The presence of cotton and sebum components on the Raes samples is not precluded.
Fig. 4.16. F TIR of “What appeared to be a thin fragment of crust”, green curve = “crust”, black curve = “linen standard”, 2008 presentation of Villarreal ©R. Breault, Shroud of Turin Education Project Inc. all the large piece of crust “may be dominated by embedded fibers”.°” Also, all large peaks of the Raes/radiocarbon and main Shroud non-image FTIRs can be assigned to linen, starch and alizarin/purpurin. The presence of cotton and sebum components on the Raes samples is not precluded.
carboxylic acids), and that of the C=O groups in conjugated structures only carboxylic acid salts (mentioned by Adler) and aromatic compounds have C=O wavenumbers at 1600 cm”.
carboxylic acids), and that of the C=O groups in conjugated structures only carboxylic acid salts (mentioned by Adler) and aromatic compounds have C=O wavenumbers at 1600 cm”.
Fig. 4.17. Comparison of ~1600 (yellow arrows) and ~1650 cm" (brown arrows) bands in white (blue curve B) and heat-yellowed (red curve A) linen fibers and Shroud non-image, image and scorch fibers. Linen details from fig. 4.12, FTIR 1500-1780 cm", mirrored upside-down (Moroni’s 1993 presentation ©R. Breault®’’); Shroud details from fig. 4.5, FTIR 1500-2600 cm" (Adler, Updating recent studies on the Shroud of Turin, 1996, ©ACS °"°) (its strongest band is at 1670-1690,°"* probably due to the aldehyde group, but this group would be lost in polymerization) and/or there is simply more water between the scorched (broken and degraded) cellulose chains. Also the high and broad ca. 1600 band of the scorched fibers may contain the strong 1604 cm" band of hydroxymethylfurfural derivatives®™*.
Fig. 4.17. Comparison of ~1600 (yellow arrows) and ~1650 cm" (brown arrows) bands in white (blue curve B) and heat-yellowed (red curve A) linen fibers and Shroud non-image, image and scorch fibers. Linen details from fig. 4.12, FTIR 1500-1780 cm", mirrored upside-down (Moroni’s 1993 presentation ©R. Breault®’’); Shroud details from fig. 4.5, FTIR 1500-2600 cm" (Adler, Updating recent studies on the Shroud of Turin, 1996, ©ACS °"°) (its strongest band is at 1670-1690,°"* probably due to the aldehyde group, but this group would be lost in polymerization) and/or there is simply more water between the scorched (broken and degraded) cellulose chains. Also the high and broad ca. 1600 band of the scorched fibers may contain the strong 1604 cm" band of hydroxymethylfurfural derivatives®™*.
Cold water spreading in the starched-washed-and-madder-dyed linen within a minute between calcium and linen, assumed to exist on the Shroud by Heller and Adler.°* So, also in th GBHA test, it is uncertain to which extent calcium actually contributed to the positive test result. The water that formed the big diamond shaped waterstains, did not irreversibly decolour the inside of the stains visibly. So, the original water of these stains probably was not (strongly) alkaline o acidic. Rogers showed that fibers of a madder-dyed thread from the Raes corner still looked yellow brown through the microscope, when mounted in water.°” An experiment showed that whe demineralized water at room temperature is sucked into a pale yellow, starched, hot-water-washec madder-dyed piece of linen, the waterstain is only a bit deeper yellow while wet, and, after drying does not yield a different color than the background, but only perhaps a little lighter hue (fig. 4.18).
Cold water spreading in the starched-washed-and-madder-dyed linen within a minute between calcium and linen, assumed to exist on the Shroud by Heller and Adler.°* So, also in th GBHA test, it is uncertain to which extent calcium actually contributed to the positive test result. The water that formed the big diamond shaped waterstains, did not irreversibly decolour the inside of the stains visibly. So, the original water of these stains probably was not (strongly) alkaline o acidic. Rogers showed that fibers of a madder-dyed thread from the Raes corner still looked yellow brown through the microscope, when mounted in water.°” An experiment showed that whe demineralized water at room temperature is sucked into a pale yellow, starched, hot-water-washec madder-dyed piece of linen, the waterstain is only a bit deeper yellow while wet, and, after drying does not yield a different color than the background, but only perhaps a little lighter hue (fig. 4.18).
Same pale yellow dried linen beside white linen, 2.5 hours after wetting, by two different cameras
Same pale yellow dried linen beside white linen, 2.5 hours after wetting, by two different cameras
that had been starched three days ago, and each piece was immersed in an unheated bath of the yellow dye for about 30 s, and then left to dry horizontally on a plate, indoors in the shade.
that had been starched three days ago, and each piece was immersed in an unheated bath of the yellow dye for about 30 s, and then left to dry horizontally on a plate, indoors in the shade.
Fig. 4.21. Cotton cheesecloth dyed with yellow acidic madder root extract. A: Both just dyed. Left piece: not starched, right piece: starched. B: Same pieces of cloth, 9 hours after dyeing. C: Same pieces of cloth plus two controls (top left: not starched, top right: starched), 12 hours after dyeing ©AvdH Although both the starched and the not-starched piece had turned yellow by dyeing, only the not- starched piece of cloth slowly turned pink (fig. 4.20), perhaps because the dyestuffs were deprotonated while binding to the linen fibers. Apparently, the slightly acidic starch coating prevented the reddening of the dye on the starched piece of cloth. A similar difference between starched and not-starched cotton, on dyeing with yellow madder dye, was observed (fig. 4.21). In another experiment, a piece of bleached and unbleached linen and a piece of cotton were immersed in vinegar first, and then, while still wet, immersed in yellow madder dye. All pieces remained yellow, except at the tips of a few corner threads.
Fig. 4.21. Cotton cheesecloth dyed with yellow acidic madder root extract. A: Both just dyed. Left piece: not starched, right piece: starched. B: Same pieces of cloth, 9 hours after dyeing. C: Same pieces of cloth plus two controls (top left: not starched, top right: starched), 12 hours after dyeing ©AvdH Although both the starched and the not-starched piece had turned yellow by dyeing, only the not- starched piece of cloth slowly turned pink (fig. 4.20), perhaps because the dyestuffs were deprotonated while binding to the linen fibers. Apparently, the slightly acidic starch coating prevented the reddening of the dye on the starched piece of cloth. A similar difference between starched and not-starched cotton, on dyeing with yellow madder dye, was observed (fig. 4.21). In another experiment, a piece of bleached and unbleached linen and a piece of cotton were immersed in vinegar first, and then, while still wet, immersed in yellow madder dye. All pieces remained yellow, except at the tips of a few corner threads.
Fig. 4.24. “(a) Vis-FOR spectra obtained for some red or pink (dotted line), yellow (dashed line) and orange-red (solid line) areas on the historical embroidered cloth. (b) Vis-FOR spectra obtained for some blue (solid line), blue green (dashed line) and green (dotted line) areas on the historical embroidered cloth.” ©Elsevier®”
Fig. 4.24. “(a) Vis-FOR spectra obtained for some red or pink (dotted line), yellow (dashed line) and orange-red (solid line) areas on the historical embroidered cloth. (b) Vis-FOR spectra obtained for some blue (solid line), blue green (dashed line) and green (dotted line) areas on the historical embroidered cloth.” ©Elsevier®”
Fig. 4.25. “Typical raw fluorescence scan (point B3A — clear)” of the Shroud ©OSA”’
Fig. 4.25. “Typical raw fluorescence scan (point B3A — clear)” of the Shroud ©OSA”’
Fig. 4.26. Smoothed fluorescence curves of four clear areas of the Shroud ©OSA’”’
Fig. 4.26. Smoothed fluorescence curves of four clear areas of the Shroud ©OSA’”’
Bier Fig. 4.27. Fluorescence ¢ of lignin- rich pulp’”” (public domain)
Bier Fig. 4.27. Fluorescence ¢ of lignin- rich pulp’”” (public domain)
fluorescence under two 770 nm photons of lignin in cell wall of bagasse fibers, normalized at 478 nm a) untreated b) acidic treatment (H2S04 1%) c) alkali treatment (NaOH 2%)
fluorescence under two 770 nm photons of lignin in cell wall of bagasse fibers, normalized at 478 nm a) untreated b) acidic treatment (H2S04 1%) c) alkali treatment (NaOH 2%)
Just dyed. top: not-starched linen, bottom: starched linen, leftmost: controls were shielded with a UV filter (Hoya L-42’™*, as in Miller and Pellicori’s fluorescence photograpy out the Wood lamp (peak intensity at ca. 365 nm) was used without an extra visible-light shield an apparently emits a visible blue component, as shown by its specular reflectance from the white plat fig. 4.30).’”° Yellow fluorescence is hardly picked up by the camera, especially from a distance, fc 1 bright green yellow fluorescence of a yellow madder dye in a glass jar is hardly seen by the camet (fig. 4.31), but is clearly seen by the eye. Because of this blue-leak from the source and the variatio in color through variation in distance and the use of a digital camera instead of an analogue fil camera, the colors in the UV photos of this paper can not be directly compared to the colors of th official, doubly shielded, UV-fluorescence photos of Miller and Pellicori’s article. So, it is difficu to estimate which of the different kinds of madder root extract best fits the Shroud, also because th Shroud has naturally aged and the shown experimentally dyed pieces have not. Yet, because of tk many possible fluorescence variations shown in the experiment, a madder extract that would t Sonsistent with the Shroud’s colors probably does exist. Besides, for some reason, various online UV or UV-fluorescence photos of the Shroud show man different colors of the Shroud background areas: rather blue (chest — Weaver and Adler), green (che and wrist a.o., Miller and Pellicori, cf. fig. 4.2 and 5.3), yellow (chest and wrist and forehead an oetween head images — Jackson videoed by Breault, wrist —Rogers, fig. 2.30), orange (Raes corner
Just dyed. top: not-starched linen, bottom: starched linen, leftmost: controls were shielded with a UV filter (Hoya L-42’™*, as in Miller and Pellicori’s fluorescence photograpy out the Wood lamp (peak intensity at ca. 365 nm) was used without an extra visible-light shield an apparently emits a visible blue component, as shown by its specular reflectance from the white plat fig. 4.30).’”° Yellow fluorescence is hardly picked up by the camera, especially from a distance, fc 1 bright green yellow fluorescence of a yellow madder dye in a glass jar is hardly seen by the camet (fig. 4.31), but is clearly seen by the eye. Because of this blue-leak from the source and the variatio in color through variation in distance and the use of a digital camera instead of an analogue fil camera, the colors in the UV photos of this paper can not be directly compared to the colors of th official, doubly shielded, UV-fluorescence photos of Miller and Pellicori’s article. So, it is difficu to estimate which of the different kinds of madder root extract best fits the Shroud, also because th Shroud has naturally aged and the shown experimentally dyed pieces have not. Yet, because of tk many possible fluorescence variations shown in the experiment, a madder extract that would t Sonsistent with the Shroud’s colors probably does exist. Besides, for some reason, various online UV or UV-fluorescence photos of the Shroud show man different colors of the Shroud background areas: rather blue (chest — Weaver and Adler), green (che and wrist a.o., Miller and Pellicori, cf. fig. 4.2 and 5.3), yellow (chest and wrist and forehead an oetween head images — Jackson videoed by Breault, wrist —Rogers, fig. 2.30), orange (Raes corner
Same pieces, 4 days after dyeing
Same pieces, 4 days after dyeing
Same pieces in UV light, photo taken through 2.5 mm thick Hoya L-42 UV filter, no blue-light filter in front of Wood lamp, 35 days after dyeing
Same pieces in UV light, photo taken through 2.5 mm thick Hoya L-42 UV filter, no blue-light filter in front of Wood lamp, 35 days after dyeing
Fig. 4.30. Specular reflectance of blue light from a white plate; photo lit with ~365 nm Wood lamy unshielded with an extra blue-light filter and photographed through a 2.5 mm thick Hoya L-42 U} filter CAvdH Fig. 4.29. (above) Dyeing pieces of linen with different madder root extracts. Dyes from left to right: 1. no dye (control), 2. root powder stirred in water at room temperature for ca. 2 h, then filtered through brown filter paper, then acidified, 3. root powder stirred in hot water for ca. 45 min, then filtered through brown filter paper, then acidified, 4. root powder extracted as tea with boiling water, then spontaneously fermented, then acidified, 5. root powder extracted as tea with boiling water then acidified and stored. All dyes had a pH < 4. ©AvdH
Fig. 4.30. Specular reflectance of blue light from a white plate; photo lit with ~365 nm Wood lamy unshielded with an extra blue-light filter and photographed through a 2.5 mm thick Hoya L-42 U} filter CAvdH Fig. 4.29. (above) Dyeing pieces of linen with different madder root extracts. Dyes from left to right: 1. no dye (control), 2. root powder stirred in water at room temperature for ca. 2 h, then filtered through brown filter paper, then acidified, 3. root powder stirred in hot water for ca. 45 min, then filtered through brown filter paper, then acidified, 4. root powder extracted as tea with boiling water, then spontaneously fermented, then acidified, 5. root powder extracted as tea with boiling water then acidified and stored. All dyes had a pH < 4. ©AvdH
Fig. 4.31. Bright green yellow fluorescence of pale yellow madder dye in a glass jar is clearly seen by the eye but hardly seen by the camera from a distance (both through a UV filter). The photos are ‘as-is’ and brightness-enhanced, respectively. The dye was extracted by heating plus stirring an aqueous suspension of madder root powder for 45 min, and after it had cooled down and spontaneously fermented, it was acidified further by adding vinegar. CAvdH
Fig. 4.31. Bright green yellow fluorescence of pale yellow madder dye in a glass jar is clearly seen by the eye but hardly seen by the camera from a distance (both through a UV filter). The photos are ‘as-is’ and brightness-enhanced, respectively. The dye was extracted by heating plus stirring an aqueous suspension of madder root powder for 45 min, and after it had cooled down and spontaneously fermented, it was acidified further by adding vinegar. CAvdH
had much more decoloring effect on starched linen than on not-treated pure linen (see fig. 4.32 and 4.33).
had much more decoloring effect on starched linen than on not-treated pure linen (see fig. 4.32 and 4.33).
If an acidic madder extract on a retrograded acidic starch film is applied to a linen cloth, it would probably also be more susceptible to oxidation and decoloration by the ozone, heat and light that accompany a corona discharge, which would allow for more gradation in areal image density before a cloth is burnt. Alizarin and purpurin are antioxidants,”° and “reducing agents”, which means that they easily get oxidized.”’ Alizarin dusts even “may form an explosive mixture with air, and any source of ignition, i.e. flame or spark, will cause fire or explosion. ... Avoid contamination with oxidizing agents i.e. nitrates, oxidizing acids, chlorine bleaches, pool chlorine etc. as ignition may result.”
If an acidic madder extract on a retrograded acidic starch film is applied to a linen cloth, it would probably also be more susceptible to oxidation and decoloration by the ozone, heat and light that accompany a corona discharge, which would allow for more gradation in areal image density before a cloth is burnt. Alizarin and purpurin are antioxidants,”° and “reducing agents”, which means that they easily get oxidized.”’ Alizarin dusts even “may form an explosive mixture with air, and any source of ignition, i.e. flame or spark, will cause fire or explosion. ... Avoid contamination with oxidizing agents i.e. nitrates, oxidizing acids, chlorine bleaches, pool chlorine etc. as ignition may result.”
aIT7.1. Dyestuffs such as alizarin and purpurin were not mentioned in the results of the Shroud’s PMS- analysis at all, not even in the results of the ample material from the Raes sample, even though the dye had been found by wet microchemical analysis on Raes threads.*'’ This means that the PMS method that was used probably was not capable of detecting these carbohydrate dyestuffs. Rogers’ PMS paper reads “We wanted to see traces of materials that were not carbohydrates. ... Since we desired detection sensitivity rather than high resolution, we used a machine with moderate resolution, chemical ionization, and high sensitivity. ... It did not detect any unexpected pyrolysis fragments that indicated any Shroud materials other than carbohydrates.”*!* So, perhaps there were PMS signals of pyrolysis products of lignin or vanillin or alizarin or purpurin that were either not “unexpected” or not recognized as such. After all. the fluorescence snectra of the Shroud’s non-imase jimagce and «ccorch areas have the 4.3. Not pectin or microbial bioplastic coating
aIT7.1. Dyestuffs such as alizarin and purpurin were not mentioned in the results of the Shroud’s PMS- analysis at all, not even in the results of the ample material from the Raes sample, even though the dye had been found by wet microchemical analysis on Raes threads.*'’ This means that the PMS method that was used probably was not capable of detecting these carbohydrate dyestuffs. Rogers’ PMS paper reads “We wanted to see traces of materials that were not carbohydrates. ... Since we desired detection sensitivity rather than high resolution, we used a machine with moderate resolution, chemical ionization, and high sensitivity. ... It did not detect any unexpected pyrolysis fragments that indicated any Shroud materials other than carbohydrates.”*!* So, perhaps there were PMS signals of pyrolysis products of lignin or vanillin or alizarin or purpurin that were either not “unexpected” or not recognized as such. After all. the fluorescence snectra of the Shroud’s non-imase jimagce and «ccorch areas have the 4.3. Not pectin or microbial bioplastic coating
Table 9. Comparison of properties of the Shroud, madder and Saponaria
Table 9. Comparison of properties of the Shroud, madder and Saponaria
Fig. 3 Absorption (a) and fluorescence (A,,.=357 nm, isosbestic point) (4) spectra of AP at pH values that correspond to the neutral form (/, pH=2), to the monoanion (2, pH=8) and to the di-anion (3, pH=12) in methanol—water (1/2 v/v) solutions. /nsert: spectrophoto- metric [Agnalysis=273 (open circle) and 298 (filled circle) nm] and fluorimetric [Agx¢=357 nm and Agn=472 nm (filled square)| titration curves
Fig. 3 Absorption (a) and fluorescence (A,,.=357 nm, isosbestic point) (4) spectra of AP at pH values that correspond to the neutral form (/, pH=2), to the monoanion (2, pH=8) and to the di-anion (3, pH=12) in methanol—water (1/2 v/v) solutions. /nsert: spectrophoto- metric [Agnalysis=273 (open circle) and 298 (filled circle) nm] and fluorimetric [Agx¢=357 nm and Agn=472 nm (filled square)| titration curves
WY ivilli a tGhoewty aBAULIaAUaUIY Ola Yi May BNE MRE EE ARGUANELY Gnly ARMREEE AEE DEE) AWN methemoglobin (crystals), amorphous acid heme dimer precipitate and heme-madder lake. Th amorphous insoluble heme precipitate would remain on the cloth longest, and the a-z heme dimer madder lake would simply be a part of the cloth’s madder coating. That blood is able to form stains on starched and madder-dyed linen that are pinkish and mor colorfast than bloodstains on pure linen, has already been shown in experiments represented in fig 2.46 and 2.47. Another experiment, in which fresh whole blood was acidified by adding an aqueou vinegar solution of pH 5.5 - 6 and then was dropped on pure and starched-(not-washed)-and-madder dyed linen (and then smeared out on the dyed piece), showed that the stain on the pure linen turne brownish pink but the stain on the dyed linen remained a bit more red (fig. 5.1). Here must be note: that these new stains of artificially acidified — and thus diluted and contaminated — fresh norma blood can not directly be compared to old stains of authentic postmortem acidemic blood. Also thi simple weave of this linen is different from the weave of the Shroud.
WY ivilli a tGhoewty aBAULIaAUaUIY Ola Yi May BNE MRE EE ARGUANELY Gnly ARMREEE AEE DEE) AWN methemoglobin (crystals), amorphous acid heme dimer precipitate and heme-madder lake. Th amorphous insoluble heme precipitate would remain on the cloth longest, and the a-z heme dimer madder lake would simply be a part of the cloth’s madder coating. That blood is able to form stains on starched and madder-dyed linen that are pinkish and mor colorfast than bloodstains on pure linen, has already been shown in experiments represented in fig 2.46 and 2.47. Another experiment, in which fresh whole blood was acidified by adding an aqueou vinegar solution of pH 5.5 - 6 and then was dropped on pure and starched-(not-washed)-and-madder dyed linen (and then smeared out on the dyed piece), showed that the stain on the pure linen turne brownish pink but the stain on the dyed linen remained a bit more red (fig. 5.1). Here must be note: that these new stains of artificially acidified — and thus diluted and contaminated — fresh norma blood can not directly be compared to old stains of authentic postmortem acidemic blood. Also thi simple weave of this linen is different from the weave of the Shroud.
Rogers on thermal denaturation of blood on the Shroud The Shroud evidence list of 2005, i.e., of after Rogers’s death says: “A61) The blood on the TS is no denatured. Therefore both the image-formation mechanism and the 1532 fire did not involve processes that would denature the blood (Rogers 2004)”, in which the reference is to “ROGERS R Shroud Science Group communication 2003, 2004”.?”° In this communication, Rogers probably dic not make a statement about denaturation by acids, but only stated that the blood was not denaturec by simple heating (pyrolysis), a conclusion he had drawn — with referral to the image-formatior process and the fire — on account of the appearance of ‘a low-temperature emission ot hydroxyproline” in Pyrolysis/Mass Spectrometry of the Zina thread’s red spots.””’ Heller and Adler did speak of a denatured methemoglobin species on the Shroud.”
Rogers on thermal denaturation of blood on the Shroud The Shroud evidence list of 2005, i.e., of after Rogers’s death says: “A61) The blood on the TS is no denatured. Therefore both the image-formation mechanism and the 1532 fire did not involve processes that would denature the blood (Rogers 2004)”, in which the reference is to “ROGERS R Shroud Science Group communication 2003, 2004”.?”° In this communication, Rogers probably dic not make a statement about denaturation by acids, but only stated that the blood was not denaturec by simple heating (pyrolysis), a conclusion he had drawn — with referral to the image-formatior process and the fire — on account of the appearance of ‘a low-temperature emission ot hydroxyproline” in Pyrolysis/Mass Spectrometry of the Zina thread’s red spots.””’ Heller and Adler did speak of a denatured methemoglobin species on the Shroud.”
Fig. 5.3. Comparison of a small of the back area in visible light and in UV light (fluorescence). Left: visible light photo (ME 03) ©1978 Mark Evans Collection, STERA, Inc.*”; right: fluorescence photo a é é . 5 7 943 (mirrored) ©Biocommunications Association, Inc. The ultimate tips of a few bloodstains that look like rivulets that flowed either across the Shroud o1 across the body look brown while the rivulet itself looks red. Beside the dorsal right foot, the small area at the outer edge of the outer bloodstain that is more brown than the rest of the stain (cf. fig. 2.1), is darker in fluorescence. The brown and, in some places, pinkish off-elbow stain” is not or the fluorescence photograph, but the trail leading to it seems just as dark as the bloodstains on the arm. At the small of the back, the brown side tip of the dense blood at the end of a blood rivulet is lighter than the dense red tip beside it in visible light, but just as dark in the fluorescence photo (fig. 5.3). So, these brown stains are not mainly serum, which would have been lighter in fluorescence. Perhaps at these ultimate tips there was a small pool of wet blood, which clotted in the Shroud before most of its liquid could drain away through the Shroud to the bier. This clot in the Shroud woulc contain red blood cells in a fibrin mesh, and therefore would retain most of these cells, in contrast tc stains mainly made by hemolysate of clots on the body and of thin filtered rivulets. The contents o1 these cells would not get into contact with madder dye and therefore would denature to browr hemichrome or heme jiict a¢ blood in ordinary hlaodsctaing does.
Fig. 5.3. Comparison of a small of the back area in visible light and in UV light (fluorescence). Left: visible light photo (ME 03) ©1978 Mark Evans Collection, STERA, Inc.*”; right: fluorescence photo a é é . 5 7 943 (mirrored) ©Biocommunications Association, Inc. The ultimate tips of a few bloodstains that look like rivulets that flowed either across the Shroud o1 across the body look brown while the rivulet itself looks red. Beside the dorsal right foot, the small area at the outer edge of the outer bloodstain that is more brown than the rest of the stain (cf. fig. 2.1), is darker in fluorescence. The brown and, in some places, pinkish off-elbow stain” is not or the fluorescence photograph, but the trail leading to it seems just as dark as the bloodstains on the arm. At the small of the back, the brown side tip of the dense blood at the end of a blood rivulet is lighter than the dense red tip beside it in visible light, but just as dark in the fluorescence photo (fig. 5.3). So, these brown stains are not mainly serum, which would have been lighter in fluorescence. Perhaps at these ultimate tips there was a small pool of wet blood, which clotted in the Shroud before most of its liquid could drain away through the Shroud to the bier. This clot in the Shroud woulc contain red blood cells in a fibrin mesh, and therefore would retain most of these cells, in contrast tc stains mainly made by hemolysate of clots on the body and of thin filtered rivulets. The contents o1 these cells would not get into contact with madder dye and therefore would denature to browr hemichrome or heme jiict a¢ blood in ordinary hlaodsctaing does.
Fig. 5.4. Streak-like pink scourge mark on right calve at location 1FB of STURP’s tape sample map. Photo by HALTADEFINIZIONE® IMAGE BANK - Copyright Arcidiocesi di Torino”*
Fig. 5.4. Streak-like pink scourge mark on right calve at location 1FB of STURP’s tape sample map. Photo by HALTADEFINIZIONE® IMAGE BANK - Copyright Arcidiocesi di Torino”*
*“ Used, with permission, from the Shroud 2.0 application made by Haltadefinizione, downloadable from http://www.haltadefinizione.com/en/the-shroud. Note that for the Haltadefinizione photography “The lighting system was especially designed to filter any harmful radiation to the cloth, but most of all special attention was given to the calibration of the spectrum, which helped faithfully reproduce the actual color and fabric of the Shroud image.” http://www.haltadefinizione.com/en/the-shroud 945 T Tead unth narmicainan fram tha Cheaid 9 fh annliiratian made hv Laltadafiniginnea Anuminadahlia feam
*“ Used, with permission, from the Shroud 2.0 application made by Haltadefinizione, downloadable from http://www.haltadefinizione.com/en/the-shroud. Note that for the Haltadefinizione photography “The lighting system was especially designed to filter any harmful radiation to the cloth, but most of all special attention was given to the calibration of the spectrum, which helped faithfully reproduce the actual color and fabric of the Shroud image.” http://www.haltadefinizione.com/en/the-shroud 945 T Tead unth narmicainan fram tha Cheaid 9 fh annliiratian made hv Laltadafiniginnea Anuminadahlia feam
Fig. 5.6. Same dense bloodstain at the tip of a bloodrivulet in the small of the back area®”, with the black rectangle indicating the same cloth area in all photos. Top left {UE 06, adapted) and middle left (ME 03, adapted): Ol 978 Mark Evans Collection, STERA, Inc.*™*; top right (part of ME 03 as published by McCrone™*, adapted): © 1990 ACS °°’; bottom left, photo (adapted) showing faint pinkish dumbbell-shaped scourge mark, and dense bloodstain and another blood rivulet: Photo by HALTADEFINIZIONE® IMAGE BANK - Copyright Arcidiocesi di Torino””’. Composition: ©AvdH
Fig. 5.6. Same dense bloodstain at the tip of a bloodrivulet in the small of the back area®”, with the black rectangle indicating the same cloth area in all photos. Top left {UE 06, adapted) and middle left (ME 03, adapted): Ol 978 Mark Evans Collection, STERA, Inc.*™*; top right (part of ME 03 as published by McCrone™*, adapted): © 1990 ACS °°’; bottom left, photo (adapted) showing faint pinkish dumbbell-shaped scourge mark, and dense bloodstain and another blood rivulet: Photo by HALTADEFINIZIONE® IMAGE BANK - Copyright Arcidiocesi di Torino””’. Composition: ©AvdH
vidence of liquid sweat on the Shroud,”*® but Jesus’ sweat may have been just as dry as the blood of he scourge wounds at the time of burial. On the other hand, the detected Na and Cl on the reverse ide may also result from a layer of salt crystals on which Jews used to lay their dead to retard lecomposition of the body before washing and anointing and burying it.”*’ Some of the aragonite dir vas found on the left knee image, and the left knee (and more clearly the right knee) also shows a ew faint pinkish bloodstains that could be imprints of scourge wounds (fig. 5.9). So it seems at leas he knees weren’t washed in a way that removed both the dry blood flows on the knees and the dirt. f a superficial washing removed only the dry blood flows and the superficial dirt but not the dir leeper in the skin (or the clots on the wounds), then this remaining deeper dirt would not have been ransferred upward into the Shroud either. So, a washing scenario for the transferral of the scourge narks seems unlikely.
vidence of liquid sweat on the Shroud,”*® but Jesus’ sweat may have been just as dry as the blood of he scourge wounds at the time of burial. On the other hand, the detected Na and Cl on the reverse ide may also result from a layer of salt crystals on which Jews used to lay their dead to retard lecomposition of the body before washing and anointing and burying it.”*’ Some of the aragonite dir vas found on the left knee image, and the left knee (and more clearly the right knee) also shows a ew faint pinkish bloodstains that could be imprints of scourge wounds (fig. 5.9). So it seems at leas he knees weren’t washed in a way that removed both the dry blood flows on the knees and the dirt. f a superficial washing removed only the dry blood flows and the superficial dirt but not the dir leeper in the skin (or the clots on the wounds), then this remaining deeper dirt would not have been ransferred upward into the Shroud either. So, a washing scenario for the transferral of the scourge narks seems unlikely.
Fig. 6.1. Absorbance of heme and of nitrosoheme made of hemin and myoglobin, respectively OAC!
Fig. 6.1. Absorbance of heme and of nitrosoheme made of hemin and myoglobin, respectively OAC!
Fig. 6.3. FTIR spectrum after photooxidation of nitrosoheme made of hemin ©4cs'*”
Fig. 6.3. FTIR spectrum after photooxidation of nitrosoheme made of hemin ©4cs'*”
A general objection against all painted-blood hypotheses is that they do not explain the presence of separate serum on the Shroud (see 2.2), such as probably present in the fluorescence halo at the tip o1 the wrist bloodstain (unless the “blood paint’ was used to touch up authentic bloodstains). When, as during painting, a drop of fresh blood is left to dry on a horizontal cloth with interstices through which it reaches the reverse side, as on the Shroud, no separate serum ring would be produced around the bloodstain (see fig. 6.4 : in pure linen on a glass plate, such a stain does not change shape after very rapidly attaining its maximum shape); the serum would rather drain down to the reverse side. On a vertical cloth, painted -on blood would drain down inside the cloth, and if any serum borders formed (which does not happen in relatively loosely woven pure linen, see fig. 6.5), they would probably all be on the same side of the bloodstains, instead of on different sides, such as on the Shroud lateral of the wrist bloodstain, and seemingly above and beside and beneath the chest bloodstain.
A general objection against all painted-blood hypotheses is that they do not explain the presence of separate serum on the Shroud (see 2.2), such as probably present in the fluorescence halo at the tip o1 the wrist bloodstain (unless the “blood paint’ was used to touch up authentic bloodstains). When, as during painting, a drop of fresh blood is left to dry on a horizontal cloth with interstices through which it reaches the reverse side, as on the Shroud, no separate serum ring would be produced around the bloodstain (see fig. 6.4 : in pure linen on a glass plate, such a stain does not change shape after very rapidly attaining its maximum shape); the serum would rather drain down to the reverse side. On a vertical cloth, painted -on blood would drain down inside the cloth, and if any serum borders formed (which does not happen in relatively loosely woven pure linen, see fig. 6.5), they would probably all be on the same side of the bloodstains, instead of on different sides, such as on the Shroud lateral of the wrist bloodstain, and seemingly above and beside and beneath the chest bloodstain.
Fig. 6.5. Vertical linen stained with fresh whole blood, at 23-24 °C, 60-70% rel. humidity. A: linen at ~85° from table, blood falling past cloth. B: linen ~70° from table, bloody fingertip briefly touching one point of the cloth (left), blood falling on cloth (right). Last photos: Wood lamp and Hoya L-42 filter. ©CAvdH
Fig. 6.5. Vertical linen stained with fresh whole blood, at 23-24 °C, 60-70% rel. humidity. A: linen at ~85° from table, blood falling past cloth. B: linen ~70° from table, bloody fingertip briefly touching one point of the cloth (left), blood falling on cloth (right). Last photos: Wood lamp and Hoya L-42 filter. ©CAvdH
fluorescence,’ unless the paint was used to touch up real bloodstains. Yet, if a pure iron-madder ake was painted on cloth, its red fluorescence would not be quenched by heme aggregate deposits on op of it, and the painted bloodstains would probably fluoresce stronger than the non-image (yellow madder-dyed) background. This is not the case for the Shroud. Also, madder lake paint consists of particles in a binder (fig. 6.6) and therefore can not explain the presence of the smoothly purplish colored fibers from the side stain area (fig. 2.49). Painted-on madder dye, on the other hand, can not explain the presence of free blood globs, even yielding an FTIR spectrum resembling that of madder ake (fig. 2.21 and 2.22), unless it was painted on authentic heme stains.
fluorescence,’ unless the paint was used to touch up real bloodstains. Yet, if a pure iron-madder ake was painted on cloth, its red fluorescence would not be quenched by heme aggregate deposits on op of it, and the painted bloodstains would probably fluoresce stronger than the non-image (yellow madder-dyed) background. This is not the case for the Shroud. Also, madder lake paint consists of particles in a binder (fig. 6.6) and therefore can not explain the presence of the smoothly purplish colored fibers from the side stain area (fig. 2.49). Painted-on madder dye, on the other hand, can not explain the presence of free blood globs, even yielding an FTIR spectrum resembling that of madder ake (fig. 2.21 and 2.22), unless it was painted on authentic heme stains.
Table 10. Survey of red-color hypotheses and their congruence with Shroud bloodstain features
Table 10. Survey of red-color hypotheses and their congruence with Shroud bloodstain features
Besides the already mentioned evidence for the use of a (wooden) burial bier for the trasferral of he enshrouded body (viz. the necessity of the use of a flat wobbling plane on which the Shroud ay when blood rivulets ran across the waterresistant Shroud and a water-absorbant substrate beneath it — see 2.3.4 and 5.3), there is another indication for an authentic first-century Jewish burial, and even for the burial of Jesus. “In Biblical times persons, especially of high rank, were arrayed at burial in the garments, ornaments, and weapons which they had worn in life ... To be buried without garments was considered a disgrace ... As a token of honor, it was customary to cast the most costly garments and ornaments upon the bier of a dear relative or friend ... (Ket. 8b; M. K. 27b).”'°®° Beneath the beard of the body image there seems to be the image of a flat, more or less oval object (fig. 7.1). Height displays based on the grey scale values of (the negative of) a Shroud photo show the flatness of this object and some smaller protruding shapes on its flat surface (fig. 7.2 and 7.3). It seems to be either a flat and rather angular and seemingly unconnected part of the beard — a kind of Zeus beard in two parts — or else a distinct object that lay on the chest of the body. The color photography of Haltadefinizione shows that on the lower edge of this object there is the pink color that also constitutes the scourge marks and bloodstains (fig. 7.4 and 7.5).'°*’ This means that there was blood on the edge of the object.
Besides the already mentioned evidence for the use of a (wooden) burial bier for the trasferral of he enshrouded body (viz. the necessity of the use of a flat wobbling plane on which the Shroud ay when blood rivulets ran across the waterresistant Shroud and a water-absorbant substrate beneath it — see 2.3.4 and 5.3), there is another indication for an authentic first-century Jewish burial, and even for the burial of Jesus. “In Biblical times persons, especially of high rank, were arrayed at burial in the garments, ornaments, and weapons which they had worn in life ... To be buried without garments was considered a disgrace ... As a token of honor, it was customary to cast the most costly garments and ornaments upon the bier of a dear relative or friend ... (Ket. 8b; M. K. 27b).”'°®° Beneath the beard of the body image there seems to be the image of a flat, more or less oval object (fig. 7.1). Height displays based on the grey scale values of (the negative of) a Shroud photo show the flatness of this object and some smaller protruding shapes on its flat surface (fig. 7.2 and 7.3). It seems to be either a flat and rather angular and seemingly unconnected part of the beard — a kind of Zeus beard in two parts — or else a distinct object that lay on the chest of the body. The color photography of Haltadefinizione shows that on the lower edge of this object there is the pink color that also constitutes the scourge marks and bloodstains (fig. 7.4 and 7.5).'°*’ This means that there was blood on the edge of the object.
Fig. 7.2. Height display of isolines of gray scale values of negative photo of the Shroud face — settings set to show the overall flatness of the object beneath the chin (original Shroud photo'°” ©1978 Barrie M. Schwortz Collection, STERA, Inc.; height display ©AvdH
Fig. 7.2. Height display of isolines of gray scale values of negative photo of the Shroud face — settings set to show the overall flatness of the object beneath the chin (original Shroud photo'°” ©1978 Barrie M. Schwortz Collection, STERA, Inc.; height display ©AvdH
The question is whether this bloodstain, which looks like a smear, could have been present on the edge of the beard. There are blood rivulets on the image of the hair, but before image formation this blood may have been on the skin of the front and sides of the face.'° Baima Bollone wrote that the bloodstains on the forehead and hair have borders that are more coloured than the centres, '°"* which according to Barbet is typical for blood clots formed on the skin.'° The blood on the edge of the oval object has the aspect of a smear on a solid edge, not of blood soaked into the usually frayed and fluffy end of a beard. This seems evidence in support of the presence of a so-called ‘petalon’, a gold oval ornament of a member of the Jewish Great Sanhedrin between ca. 6 and 70 AD, engraved I X Y
The question is whether this bloodstain, which looks like a smear, could have been present on the edge of the beard. There are blood rivulets on the image of the hair, but before image formation this blood may have been on the skin of the front and sides of the face.'° Baima Bollone wrote that the bloodstains on the forehead and hair have borders that are more coloured than the centres, '°"* which according to Barbet is typical for blood clots formed on the skin.'° The blood on the edge of the oval object has the aspect of a smear on a solid edge, not of blood soaked into the usually frayed and fluffy end of a beard. This seems evidence in support of the presence of a so-called ‘petalon’, a gold oval ornament of a member of the Jewish Great Sanhedrin between ca. 6 and 70 AD, engraved I X Y
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BiochemistryPhysiologyNear Eastern ArchaeologyPhysicsChemistryHematologyFluorescence SpectroscopyForensic ScienceHistory of TextilesSpectroscopy
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