SITE SELECTIVITY IN THE GLYCATION OF ALPHA-A-CRYSTALLIN AND ALPHA-B-CRYSTALLIN BY GLUCOSE

被引：30

作者：

ABRAHAM, EC ^{[1
]}

CHERIAN, M ^{[1
]}

SMITH, JB ^{[1
]}

机构：

[1] PURDUE UNIV,DEPT MED CHEM & PHARMACOGNOSY,W LAFAYETTE,IN 47907

来源：

BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS | 1994年 / 201卷 / 03期

关键词：

D O I：

10.1006/bbrc.1994.1866

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：

We determined the site selectivity of glycation by glucose (glucosylation) in alpha A- and alpha B-crystallins using two independent approaches. HPLC purified C-14-glucose labeled chymotryptic peptides and affinity chromatography/HPLC purified fully glycated peptides were identified by FAB-MS. Lys 11 and 78 of alpha A-crystallin and Lys 90 and/or 92 of alpha B-crystallin were the fast reacting sites of glucosylation. (C) 1994 Academic Press, Inc.

引用

页码：1451 / 1456

页数：6

共 18 条

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