MODEL FOR THE ARCHITECTURE OF ALPHA-CRYSTALLIN

被引：68

作者：

BINDELS, JG

SIEZEN, RJ

HOENDERS, HJ

机构：

[1] Department of Biochemistry, University of Nijmegen, Nijmegen

来源：

OPHTHALMIC RESEARCH | 1979年 / 11卷 / 5-6期

关键词：

Calf lens α-crystallin; Chemical cross-linking; High molecular weight crystallin aggregates; Limited proteolysis; Postsynthetic modifications; Quaternary structure; Sulfhydryl group modification; Urea dissociation;

D O I：

10.1159/000265048

中图分类号：

R77 [眼科学];

学科分类号：

100212 ;

摘要：

Knowledge of the quaternary structure of α-crystallin is required to understand the age-dependent superaggregation processes, eventually leading to lens opacification. Different approaches, e.g. sulfhydryl modification, chemical cross-linking, limited proteolysis and dissociation studies revealed new information, providing a basis for further studies of aging and higher-order structures. A model for the architecture of native α-crystallin from calf lens cortex, featuring subunit arrangement and surface exposure, will be presented. © 1979 S. Karger AG, Basel.

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页码：441 / 452

页数：12

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