Dependence of actomyosin ATPase activity on ionic strength and its modification by thiol group substitution
Author:
Publisher
Wiley
Subject
Cell Biology,Genetics,Molecular Biology,Biochemistry,Structural Biology,Biophysics
Link
http://onlinelibrary.wiley.com/wol1/doi/10.1016/0014-5793(71)80367-8/fullpdf
Reference5 articles.
1. Calcium and muscle contraction
2. Natural tropomyosin as a physiological inhibitor of the contractile activity of actomyosin
3. A Second Type of the Inhibitory Effect of Magnesium on Superprecipitation and on ATPase of Myosin B, and Its Reversal by pChloromercuribenzoate and by Adenosine Diphosphate*
4. Cardiac myofibrillar ATPase: A comparison with that of fast skeletal actomyosin in its native and in an altered conformation
5. The importance of sulfhydryl groups for the calcium-sensitive response of natural actomyosin
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1. Evidence for a role for cardiac myosin in regulating the contractile response;Archives of Biochemistry and Biophysics;1975-11
2. Dinitrophenylation of rabbit skeletal actomyosin;Biochimica et Biophysica Acta (BBA) - Protein Structure;1975-07
3. Physico-chemical studies on the light chains of myosin III. Evidence for a regulatory role of a rabbit myosin light chain;Biochemical and Biophysical Research Communications;1974-04
4. Tension in Skinned Frog Muscle Fibers in Solutions of Varying Ionic Strength and Neutral Salt Composition;Journal of General Physiology;1973-11-01
5. Molecular control mechanisms in muscle contraction.;Physiological Reviews;1973-07
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