THE SITE OF NONENZYMIC GLYCATION OF HUMAN EXTRACELLULAR-SUPEROXIDE DISMUTASE INVITRO

被引:29
作者
ADACHI, T [1 ]
OHTA, H [1 ]
HAYASHI, K [1 ]
HIRANO, K [1 ]
MARKLUND, SL [1 ]
机构
[1] UMEA UNIV HOSP, DEPT CLIN CHEM, S-90185 UMEA, SWEDEN
关键词
EXTRACELLULAR-SUPEROXIDE DISMUTASE; NONENZYMIC GLYCATION; DIABETES; HEPARIN; FREE RADICALS;
D O I
10.1016/0891-5849(92)90016-A
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
The secretory enzyme extracellular-superoxide dismutase (EC-SOD) has affinity for heparin and some other sulfated glycosaminoglycans and is in vivo bound to heparan sulfate proteoglycan. Nonenzymic glycation of EC-SOD, both in vivo and in vitro, is associated with a reduction in heparin affinity, whereas the enzymic activity is not affected. The glycation sites in EC-SOD are further studied in the present article. It is shown that modification of a few of the five lysyl residues of the subunits of the enzyme with trinitrobenzene sulfonic acid nearly abolishes the in vitro glycation susceptibility. From a chymotryptic digest of in vitro glycated EC-SOD, two peptides with affinity for boronate could be isolated. Amino acid sequence analysis showed that both encompassed the carboxyterminal end. Epsilon-Glucitol lysine was identified in both peptides at positions 211 and 212. The primary glycation sites in EC-SOD are thus lysine-211 and lysine-212 in the putative heparin-binding domain in the carboxyterminal end.
引用
收藏
页码:205 / 210
页数:6
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