AGE-DEPENDENT DEAMIDATION OF ALPHA-B-CRYSTALLIN

被引：56

作者：

GROENEN, PJTA ^{[1
]}

VANDONGEN, MJP ^{[1
]}

VOORTER, CEM ^{[1
]}

BLOEMENDAL, H ^{[1
]}

DEJONG, WW ^{[1
]}

机构：

[1] CATHOLIC UNIV NIJMEGEN,DEPT BIOCHEM,POB 9101,6500 HB NIJMEGEN,NETHERLANDS

来源：

FEBS LETTERS | 1993年 / 322卷 / 01期

关键词：

LENS; ALPHA-B-CRYSTALLIN; DEAMIDATION; RACEMIZATION; MOLECULAR AGING;

D O I：

10.1016/0014-5793(93)81113-E

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：

Bovine and human alphaB-crystallin undergo deamidation upon aging in the lens. In bovine alphaB-crystallin, the specific site of deamidation has been identified by peptide mapping after tryptic digestion. Asn-146 was found to be subject to deamidation, whereas the only other asparagine residue, at position 78, is not affected. Asn-146 is flanked at the carboxylic side by a glycyl residue. Yet, the rate of in vivo deamidation is low. In vitro studies reveal that the deamidation is accompanied by significant racemization, indicating that the deamidation proceeds via formation of a succinimide intermediate.

引用

页码：69 / 72

页数：4

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