RECOVERY OF SOME FUNCTIONAL PROPERTIES OF DETERGENT-EXTRACTED CHOLINERGIC RECEPTOR PROTEIN FROM TORPEDO-MARMORATA AFTER REINTEGRATION INTO A MEMBRANE ENVIRONMENT

被引：44

作者：

BRILEY, MS ^{[1
]}

CHANGEUX, JP ^{[1
]}

机构：

[1] INST PASTEUR,DEPT BIOL MOLEC,2528 RUE DOCTEUR ROUX,F-75724 PARIS,FRANCE

来源：

EUROPEAN JOURNAL OF BIOCHEMISTRY | 1978年 / 84卷 / 02期

关键词：

D O I：

10.1111/j.1432-1033.1978.tb12184.x

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：

The change of affinity of the acetylcholine receptor for agonists and the influence of local anaesthetics has been studied in detail in receptor‐rich membranes. These properties are changed after solubilisation by ionic detergents. A method for reproducibly reintegrating the receptor protein into a lipid environment is described. Reintegration of the receptor results in partial recovery of the binding and fluorescence properties of the membrane‐bound receptor protein. In particular, the slow affinity change caused by agonists can be recovered but not the effect of local anaesthetics on this change. The fluorescence response to cholinergic ligands of the reintegrated receptor protein labelled with quinacrine does not appear identical to that found with the native receptor‐rich membranes. It is suggested that the failure to recover the sensitivity to local anaesthetics is at the origin of the difficulties to regain functional reconstitution. Copyright © 1978, Wiley Blackwell. All rights reserved

引用

页码：429 / 439

页数：11

共 32 条

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