Effect of temperature on actin activation of heavy meromyosin ATPase
Author:
Publisher
Elsevier BV
Subject
Cell Biology,Biochemistry,Biophysics
Reference10 articles.
1. ATPase Activity of Myosin Correlated with Speed of Muscle Shortening
2. The Pre-steady State of the Myosin-Adenosine Triphosphate System
3. Die Umwandlung von Aktomyosin-ATPase in L-Myosin-ATPase durch Aktivatoren und die resultierenden Aktivierungseffekte
4. A study of the kinetics of the fibrillar adenosine triphosphatase of rabbit skeletal muscle
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1. Probing actomyosin interactions with 2,4-dinitrophenol;Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics;2005-05
2. Temperature dependence of the release of ATP hydrolysis products from the 10S conformation of smooth muscle myosin;Journal of Muscle Research and Cell Motility;1989-12
3. Butanedione Monoxime Suppresses Contraction and ATPase Activity of Rabbit Skeletal Muscle1;The Journal of Biochemistry;1989-04
4. Temperature dependence of the crossbridge cycle during unloaded shortening and maximum isometric tetanus in frog skeletal muscle;Journal of Muscle Research and Cell Motility;1986-08
5. Role of the 50-kilodalton tryptic peptide of myosin subfragment 1 as a communicating apparatus between the adenosine triphosphatase and actin binding sites;Biochemistry;1986-04-01
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