Glycation of Erythrocyte Superoxide Dismutase Reduces Its Activity(Pharmaceutical)
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Commercially available Cu, Zn superoxide dismutase (SOD) from bovine erythrocytes was purified. Purified SOD was incubated with 1 M glucose at 37℃ for 14d under sterile conditions, Nonezymatic addition of glucose to SOD molecules increased linearly until 7 d, and then increased only slightly. The enzyme activity decreased to 88% after 7d and 60% after 14d. The glycated amino acid residue is not the N-terminal α-amino group but the ε-amino group of lysine. It seems that lysine at the active center, which assists the interaction of O_2- and the SOD molecule, is affected during 14d.
- 1987-01-25
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