Characterisation of ATP binding inhibition to the sarcoplasmic reticulum Ca2+‐ATPase by thapsigargin

FEBS Letters

Dupont, Yves¹  Girardet, Jean-Luc¹  DeJesus, Florence¹ 

[1] Biophysique Moléculaire et Cellulaire, Département de Biologie Moléculaire et Structurale, Centre d'Etudes Nucléaires de Grenoble, 38041 Grenoble, France

关键词: Ca-ATPase;    Thapsigargin;    ATP;   

DOI  :  10.1016/0014-5793(93)80638-B

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

The inhibition of Ca²⁺-ATPase of sarcoplasmic reticulum by thapsigargin has been reported to be associated with a suppression of calcium binding to the high affinity transport sites. We report here that thapsigargin also acts as an inhibitor of ATP binding by reducing its apparent affinity by about two orders of magnitude. This inhibition is non-competitive indicating that thapsigargin does not bind to the ATP binding site. This is confirmed by the fact that thapsigargin binding to the Ca²⁺-ATPase does not affect the binding of 2',3'-O-(2,4,6-trinitrocyclohexadienylidene)-ATP (TNP-ATP).

【 授权许可】

Unknown