Glycation of erythrocyte superoxide dismutase reduces its activity.
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چکیده
منابع مشابه
Glycation of erythrocyte superoxide dismutase reduces its activity.
purified. Purified SOD was incubated with 1 M glucose at 37 •Ž 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 a-amino group but the s-amino group of lysine. It seems that lysine ...
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1. A simplified procedure for the preparation of highly purified human superoxide dismutase from erythrocytes was developed which avoided extremes of pH and ionic strength and the use of organic solvents; the properties of human and bovine proteins, prepared by the method, were compared. 2. Using the two dimensional electrophoretic procedure of O'Farrell, the human superoxide dismutase was foun...
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Human Cu,Zn-superoxide dismutase (Cu,Zn-SOD) undergoes site-specific and random fragmentation by non-enzymic glycosylation (glycation). Released Cu2+ from the glycated Cu,Zn-SOD probably facilitates a Fenton reaction to convert H2O2 into hydroxy radical, which then participates in the non-specific fragmentation [Ookawara et al. (1992) J. Biol. Chem. 267, 18505-18510]. In the present study, we i...
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ژورنال
عنوان ژورنال: Chemical and Pharmaceutical Bulletin
سال: 1987
ISSN: 0009-2363,1347-5223
DOI: 10.1248/cpb.35.302