Effect of C-protein on actomyosin ATPase |
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Authors: | C Moos I-nan M Feng |
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Institution: | Department of Biochemistry, State University of New York, Stony Brook, NY 11794 U.S.A. |
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Abstract: | The effect of C-protein on the actin-activated ATPase of column-purified skeletal muscle myosin has been investigated at varied ionic strength. At ionic strengths below about 0.1, C-protein is a potent inhibitor. The inhibition is not reversed by increasing the actin concentration, showing that it is caused by C-protein bound to the myosin filaments. When the ionic strength is raised above about 0.12, on the other hand, the inhibition vanishes and C-protein becomes a mild activator of the actomyosin ATPase. Both effects appear rapidly upon addition of C-protein to pre-formed myosin filaments, so C-protein probably acts by binding to the surface of the filaments. |
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Keywords: | Actomyosin ATPase C-protein Myosin (Skeletal muscle) EGTA S-1 subfragment 1 of myosin S-2 subfragment 2 of myosin |
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