INVOLVEMENT OF THE N-TERMINAL REGION IN ALPHA-CRYSTALLIN LENS MEMBRANE RECOGNITION

被引：11

作者：

IFEANYI, F ^{[1
]}

TAKEMOTO, L ^{[1
]}

机构：

[1] KANSAS STATE UNIV AGR & APPL SCI,DIV BIOL,ACKERT HALL,MANHATTAN,KS 66506

来源：

EXPERIMENTAL EYE RESEARCH | 1991年 / 53卷 / 03期

基金：

美国国家航空航天局; 美国国家卫生研究院;

关键词：

ALPHA-CRYSTALLIN BINDING; LENS MEMBRANE;

D O I：

10.1016/0014-4835(91)90234-6

中图分类号：

R77 [眼科学];

学科分类号：

100212 ;

摘要：

Previous studies have demonstrated that α-crystallin binds specifically, in a saturable manner, to lens membrane. To determine the region of the α-crystallin molecule that might be involved in this binding, native α-crystallin from the bovine lens has been treated by limited digestion with trypsin, to produce α-A molecules with an intact C-terminal region, and a nicked N-terminal region. Compared to intact α-crystallin, trypsin-treated α-crystallin binds less avidly to lens membrane, suggesting that the N-terminal region of the α-A molecule may play a key role in the recognition between lens membrane and crystallin. © 1991.

引用

页码：305 / 308

页数：4

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