CALCIUM BINDING PROPERTIES OF SARCOPLASMIC RETICULUM MEMBRANES

被引：33

作者：

COHEN, A

SELINGER, Z

机构：

[1] Departmet of Biological Chemistry, The Hebrew University of Jerusalem, Jerusalem

来源：

BIOCHIMICA ET BIOPHYSICA ACTA | 1969年 / 183卷 / 01期

关键词：

D O I：

10.1016/0005-2736(69)90126-6

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：

Sarcoplasmic reticulum from rabbit skeletal muscle demonstrates two types of ATP-independent calcium binding. About 10% of the total calcium-binding sites are very little influenced by ionic strength and are readily inactivated by trypsin proteolysis. The remaining calcium-binding sites are relatively heat stable and are not inactivated by trypsin proteolysis. Calcium binding by these sites is dependent on the ionic strength and is completely inhibited by 0.01 M MgCl2, 0.6 M KCl or 0.6 M NaCl. Total calcium-binding capacity as tested in media of low ionic strength is 50 nmoles of calcium bound per mg of sarcoplasmic reticulum protein. Both binding systems have an apparent dissociation constant of 40 μM and are not influenced by hydrolysis of the membrane phospholipids by phospholipase C. © 1969.

引用

页码：27 / &

共 23 条

[1] A SIMPLE EFFICIENT LIQUID SCINTILLATOR FOR COUNTING AQUEOUS SOLUTIONS IN A LIQUID SCINTILLATION COUNTER [J].