REGULATION OF DROSOPHILA MYOSIN ATPASE ACTIVITY BY PHOSPHORYLATION OF MYOSIN LIGHT-CHAINS .1. WILD-TYPE FLY

被引：27

作者：

TAKAHASHI, S

TAKANOOHMURO, H

MARUYAMA, K

机构：

[1] CHIBA UNIV,FAC SCI,DEPT BIOL,CHIBA 260,JAPAN

[2] TOKYO METROPOLITAN INST MED SCI,DIV BIOINFORMAT ENGN,TOKYO 113,JAPAN

来源：

COMPARATIVE BIOCHEMISTRY AND PHYSIOLOGY B-BIOCHEMISTRY & MOLECULAR BIOLOGY | 1990年 / 95卷 / 01期

关键词：

D O I：

10.1016/0305-0491(90)90267-W

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：

1. 1. Two types of myosins with phosphorylated and dephosphorylated myosin light chains were prepared from Drosophila flies. The former had ATPase (Ca2+- and Mg2+-activated) activities twice those of the latter. 2. 2. The myosin phosphorylated with crude myosin light chain kinase from flies showed ATPase (Ca2+- and Mg2+-activated) activaties twice those of the dephosphorylated myosin. 3. 3. It is suggested that phosphorylation of myosin light chains several hours after emergence stimulates myosin ATPase activity so as to facilitate the flight function of the fruitfly. © 1989.

引用

页码：179 / 181

页数：3

共 12 条

[1] TROPONIN OF ASYNCHRONOUS FLIGHT-MUSCLE [J].