THERMALLY POTENTIATED STATE FOR ACTOMYOSIN ATPASE OF RABBIT SKELETAL-MUSCLE

被引：5

作者：

GIAMBALVO, A ^{[1
]}

DREIZEN, P ^{[1
]}

机构：

[1] SUNY,DOWNSTATE MED CTR,DEPT MED,BROOKLYN,NY 11203

来源：

BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS | 1978年 / 84卷 / 01期

关键词：

D O I：

10.1016/0006-291X(78)90283-8

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：

Heat-treatment of natural actomyosin at low ionic strength in the absence of substrate results in substantial augmentation of Mg-ATPase, and minor increase of Ca-ATPase and decrease of EDTA-ATPase. Changes in Steady-state activity persist despite decrease of temperature. The effect appears to involve a thermally induced transition to a stable potentiated state for natural actomyosin. The phenomenon requires interaction between actin and myosin during heat-treatment; however, the presence of troponin and tropomyosin is needed for potentiation to be fully manifest. Thermal potentiation significantly modifies the Arrhenius behavior of actomyosin ATPase, and the augmented catalytic rate reflects a large increase of activation entropy. © 1978.

引用

页码：208 / 214

页数：7

共 10 条

[1] COOPERATION WITHIN ACTIN FILAMENT IN VERTEBRATE SKELETAL-MUSCLE [J].