Purification and characterization of myosin from wheat mitochondria

被引：1

作者：

Zhao, HP

Liu, AX

Liu, GQ ^{[1
]}

Yen, LF

机构：

[1] China Agr Univ, Coll Biol Sci, Key Lab Plant Physiol & Biochem, Minist Agr, Beijing 100094, Peoples R China

[2] Beijing Normal Univ, Coll Life Sci, Inst Cell Biol, Beijing 100875, Peoples R China

来源：

CHINESE SCIENCE BULLETIN | 2002年 / 47卷 / 04期

基金：

中国国家自然科学基金;

关键词：

myosin; mitochondria; purification; ATPase;

D O I：

10.1360/02tb9075

中图分类号：

O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];

学科分类号：

07 ; 0710 ; 09 ;

摘要：

Myosin was purified from wheat mitochondria using DE-52 anion exchange chromatography and Sephacryl S-300 gel filtration. The molecular weight of its heavy chain is about 210 ku, similar to that of muscle myosin II (205 ku), and it could be recognized by the polyclonal antibodies against human skeletal muscle myosin II. The ATPase activity of the mitochondrial myosin stimulated by F-actin from chicken muscle is 202.5 nmoles Pi/min . mg. The mitochondrial myosin could be activated by Ca2+ and was not inhibited by Ca2+ at high concentration. The results demonstrate that the myosin of wheat mitochondria shares some similarities with the skeletal muscle myosin II.

引用

页码：315 / 318

页数：4

共 21 条

[1]

Ikonen E, 1997, J CELL SCI, V110, P2155

[2] PARTIAL-PURIFICATION OF MYOSIN FROM LILY POLLEN TUBES BY MONITORING WITH INVITRO MOTILITY ASSAY [J].