ADP binds similarly to rigor muscle myofibrils and to actomyosin‐subfragment one

FEBS Letters

Adams, Patricia H.¹  Johnson, Robert E.¹ 

[1] Department of Biochemistry, University of Arizona, Tucson, AZ 85721, USA

关键词: Bovine cardiac myofibril;    Rabbit skeletal myofibril;    Actomyosin ATPase;    Mg2+;    ADP binding;    Actomyosin-subfragment one;    Cross-bridge cycle;   

DOI  :  10.1016/0014-5793(84)81067-4

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

The binding of Mg²⁺ ADP to both rabbit skeletal and bovine cardiac myofibrils has been studied at two different temperatures. In each case a single class of binding sites was observed with a binding constant very close to that reported for the analogous actomyosin-subfragment one but much weaker than that seen with the analogous myosin subfragment one alone. These findings are discussed in terms of the constraints on the myosin cross-bridges imposed by the regular array of thick and thin filaments found in myofibrils.

【 授权许可】

Unknown