THE CALCIUM ATPASE OF SARCOPLASMIC-RETICULUM IS INHIBITED BY ONE CA-2+ ION

被引：12

作者：

KHANANSHVILI, D ^{[1
]}

MYUNG, J ^{[1
]}

KOLOUCH, R ^{[1
]}

JENCKS, WP ^{[1
]}

机构：

[1] BRANDEIS UNIV,GRAD DEPT BIOCHEM,WALTHAM,MA 02254

来源：

FEBS LETTERS | 1990年 / 260卷 / 01期

关键词：

ATPase; calcium; Calcium; Inhibition;

D O I：

10.1016/0014-5793(90)80071-P

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：

Inhibition by calcium of the steady-state turnover of the calcium ATPase from sarcoplasmic reticulum of rabbit muscle follows a Hill slope of 0.8 ± 0.2 (pH 7.0, 0.1 M KCl, varying [Mg2+] and 2 μM A23187 ionophore). It is concluded that dissociation of the two Ca2+ ions from E-P·Ca2 is sequential and that the inhibition arises from the binding of one Ca2+ to A-P·Ca1. © 1990.

引用

页码：83 / 84

页数：2

共 15 条

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