PURIFICATION OF A CL--CHANNEL PROTEIN OF SARCOPLASMIC-RETICULUM BY ASSAYING THE CHANNEL ACTIVITY IN THE PLANAR LIPID BILAYER SYSTEM

被引：19

作者：

IDE, T

SAKAMOTO, H

MORITA, T

TAGUCHI, T

KASAI, M

机构：

[1] Department of Biophysical Engineering, Faculty of Engineering Science, Osaka University, Toyonaka, Osaka

来源：

BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS | 1991年 / 176卷 / 01期

关键词：

D O I：

10.1016/0006-291X(91)90886-C

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：

A Cl- channel protein of sarcoplasmic reticulum (SR) was purified by assaying the channel activity in a planar lipid bilayer system. The light fraction of SR vesicles was solubilized in CHAPS and fractionated by anion exchange, gel filtration, and affinity chromatography with concanavalin A. All fractions in each step were reconstituted into vesicles with asolectin by dialysis and their channel activities were assayed after the vesicles had been fused into a planar lipid bilayer. A 100-kDa protein, different from Ca2+-ATPase, was found to form anion channels. © 1991.

引用

页码：38 / 44

页数：7

共 14 条

[1] PURIFICATION OF TETRODOTOXIN-BINDING COMPONENT ASSOCIATED WITH VOLTAGE-SENSITIVE SODIUM CHANNEL FROM ELECTROPHORUS-ELECTRICUS ELECTROPLAX MEMBRANES [J].