Glycation of erythrocyte superoxide dismutase reduces its activity.

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Abstract
Commercially available Cu, Zn superoxide dismutase (SOD) from bovine erythrocytes was purified. Purified SOD was incubated with 1 M glucose at 37.degree. C for 14 d under sterile conditions. Nonenzymatic addition of glucose to SOD molecules increased linearly until 7 d, and then increased only slightly. The enzyme activity decreased to 88% after 7 d and 60% after 14 d. The glycated amino acid residue is not the N-terminal .alpha.-amino group but the .epsilon.-amino group of lysine. It seems that lysine at the active center, which assists the interaction of O2- and the SOD molecule, is affected during 14 d.