PRIMARY STRUCTURE OF BETA-S-CRYSTALLIN FROM HUMAN LENS

被引：15

作者：

ZARINA, S ^{[1
]}

ABBASI, A ^{[1
]}

ZAIDI, ZH ^{[1
]}

机构：

[1] UNIV KARACHI,HEJ RES INST CHEM,KARACHI 75270,PAKISTAN

来源：

BIOCHEMICAL JOURNAL | 1992年 / 287卷

关键词：

D O I：

10.1042/bj2870375

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 complete primary structure of beta(s)-crystallin from human lens is reported. The sequence was elucidated by automatic Edman degradation of tryptic and CNBr peptides. The blocked N-terminal dipeptide was identified by fast-atom-bombardment mass spectroscopy. The sequence comparison with other members of crystallin family reveals a closer relationship to human gamma-crystallin (53% identity) than with betaA3/A1 crystallin (37% identity). The structure, evolutionary characteristics and role of beta(s)-crystallin in lens are discussed.

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页码：375 / 381

页数：7

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