IMPROVED RESOLUTION OF CALF LENS BETA-CRYSTALLINS

被引：43

作者：

ASSELBERGS, FAM

KOOPMANS, M

VANVENROOIJ, WJ

BLOEMENDAL, H

机构：

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

来源：

EXPERIMENTAL EYE RESEARCH | 1979年 / 28卷 / 02期

关键词：

aggregate-size; gel electrophoresis; lens; β-crystallin;

D O I：

10.1016/0014-4835(79)90133-7

中图分类号：

R77 [眼科学];

学科分类号：

100212 ;

摘要：

Native crystallins isolated from the calf lens cortex were separated by a modified gel filtration procedure. The constituent polypeptides were then separated by gel electrophoresis. It was found, that, when gel filtration was performed in the presence of 1 m-NaCl or alternatively at room temperature, a 60 000 dalton constituent, consisting mainly of βBp, was released from βH leaving a core βH" of about 180 000 daltons. The βL fraction was partially resolved into several sizes of protein aggregates. © 1979."

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页码：223 / 228

页数：6

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