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Figure 1. Protein stainings of dioscorin without (lane 1) and with (lane 2) 2-mercaptoethanol treatment on an SDS-PAGE gel after DE-52 ion exchange column purification. M indicated the Seeblue prestained markers of SDS-PAGE; 2 wg of protein was loaded in each well.

Figure 1 Protein stainings of dioscorin without (lane 1) and with (lane 2) 2-mercaptoethanol treatment on an SDS-PAGE gel after DE-52 ion exchange column purification. M indicated the Seeblue prestained markers of SDS-PAGE; 2 wg of protein was loaded in each well.

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Figure 4. Scavenging activity of 32 kDa dioscorin against DPPH radical determined by EPR spectrometry. Sample solutions contained two different amounts of 32 kDa dioscorin [28.6 nmol (B, E) and 57 nmol (C, F)] in deionized water. The deionized water was used instead of sample solution for control experiments (A, D). Then, 10 wL of deionized water (A—C) or 10 wL of 1 M Tris-HCl buffer (pH 7.9) (D—F) was added to the sample and control solutions, and finally 250 wL of DPPH in methanol (2 mM) was added; the intensities of DPPH signals were then determined.
Figure 4. Scavenging activity of 32 kDa dioscorin against DPPH radical determined by EPR spectrometry. Sample solutions contained two different amounts of 32 kDa dioscorin [28.6 nmol (B, E) and 57 nmol (C, F)] in deionized water. The deionized water was used instead of sample solution for control experiments (A, D). Then, 10 wL of deionized water (A—C) or 10 wL of 1 M Tris-HCl buffer (pH 7.9) (D—F) was added to the sample and control solutions, and finally 250 wL of DPPH in methanol (2 mM) was added; the intensities of DPPH signals were then determined.
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EngineeringHydrogen-Ion ConcentrationPLANT PROTEINS
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