ON THE SUBSTRATE-SPECIFICITY OF ALPHA-CRYSTALLIN AS A MOLECULAR CHAPERONE

被引：80

作者：

DAS, KP

SUREWICZ, WK

机构：

[1] UNIV MISSOURI,SCH MED,DEPT OPHTHALMOL,COLUMBIA,MO 65212

[2] UNIV MISSOURI,SCH MED,DEPT BIOCHEM,COLUMBIA,MO 65212

来源：

BIOCHEMICAL JOURNAL | 1995年 / 311卷

关键词：

D O I：

10.1042/bj3110367

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：

alpha-Crystallin, the major protein of the ocular lens, acts as a molecular chaperone by preventing the thermal aggregation of proteins. However, in contrast with many other heat shock proteins, alpha-crystallin fails to protect proteins from aggregation during refolding reactions. Our results indicate that alpha-crystallin has substrate specificity different from other chaperones and recognizes specific non-native intermediates formed on the denaturation pathway only, with no affinity for intermediates formed on the refolding pathway.

引用

页码：367 / 370

页数：4

共 32 条

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