THE BINDING OF ACTIN TO PHOSPHORYLATED AND DEPHOSPHORYLATED MYOSIN

被引：28
作者：
MICHNICKA, M
KASMAN, K
KAKOL, I
机构：
来源：
BIOCHIMICA ET BIOPHYSICA ACTA | 1982年 / 704卷 / 03期
关键词：
D O I：
10.1016/0167-4838(82)90069-3
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 binding of [rabbit] actin to myosin containing phosphorylated and dephosphorylated L chains (LC2) was investigated by studying the influence of actin on Mg2+- and K+-stimulated ATPase of phosphorylated and dephosphorylated myosin and by comparing the influence of PPi on actomyosin formed from pure actin and phosphorylated or dephosphorylated myosin. The concentration of actin producing inhibition of 1/2 of myosin K+-ATPase activity was 4.1 .mu.M and 7.7 .mu.M for phoshorylated and dephosphorylated myosin, respectively. Actomyosin formed from dephosphorylated myosin dissociated at lower PPi concentration than did that from the phosphorylated form. The extrapolated values for Km obtained from studies of the influence of actin on Mg2+-ATPase activity of dephosphorylated myosin were about twice as high as for the phosphorylated form. The affinity of phosphorylated myosin for actin was significantly higher under all conditions studied.
引用
收藏
页码：470 / 475
页数：6
相关论文
共 29 条
[1]  
BARANY K, 1980, FED PROC, V39, P1547
[2]  
BARANY K, 1977, J BIOL CHEM, V252, P4752
[3]  
BARANY K, 1979, J BIOL CHEM, V254, P3617
[4]   ACTIN-MYOSIM INTERACTION - INHIBITION OF MYOSIN ADENOSINE TRIPHOSPHATASE BY ACTIN [J].
BARRON, S ;
EISENBERG, E ;
MOOS, C .
SCIENCE, 1966, 151 (3717) :1541-+
[5]   STUDIES ON KINETICS OF FORMATION AND DISSOCIATION OF ACTOMYOSIN COMPLEX [J].
FINLAYSON, B ;
LYMN, RW ;
TAYLOR, EW .
BIOCHEMISTRY, 1969, 8 (03) :811-+
[6]  
Fiske CH, 1925, J BIOL CHEM, V66, P375
[7]  
GORNALL AG, 1949, J BIOL CHEM, V177, P751
[8]   INFLUENCE OF MAGNESIUM + CALCIUM PYROPHOSPHATE CHELATES OF FREE MAGNESIUM IONS FREE CALCIUM IONS + FREE PYROPHOSPHATE IONS ON DISSOCIATION OF ACTOMYOSIN IN SOLUTION [J].
GRANICHER, D ;
PORTZEHL, H .
BIOCHIMICA ET BIOPHYSICA ACTA, 1964, 86 (03) :567-&
[9]  
IKEMOTO N, 1966, BIOCHEM Z, V345, P410
[10]  
KAKOL I, 1982, BIOCHIM BIOPHYS ACTA, V704, P437, DOI 10.1016/0167-4838(82)90065-6
123