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
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.
引用
收藏
页码:441 / 452
页数:12
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