Effect of phosphorylation on the actin-activated atpase activity of myosin |
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Authors: | A. Persechini U. Mrwa D.J. Hartshorne |
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Affiliation: | 1. Muscle Biology Group, Dept. of Nutrition and Food Science University of Arizona, Tucson, AZ. 85721 USA;2. Universität Heidelberg, II. Physiologisches Institut Heidelberg, D-6900, West Germany |
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Abstract: | ![]() The purpose of this study was to test the hypothesis that the phosphorylation of myosin is solely responsible for the activation of the Mg2+-ATPase activity of gizzard actomyosin. Using a washed natural actomyosin and a reconstituted actomyosin it was shown that phosphorylation alone caused only a slight activation of ATPase activity. Full activity was obtained only when proteins in addition to the myosin light chain kinase were added. It is evident from these results that: 1) there is no simple relationship between the extent of myosin phosphorylation and the specific Mg2+-ATPase activity of actomyosin and 2) in order for full activation by actin of the Mg2+-ATPase activity of phosphorylated myosin additional factors are required. |
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Keywords: | MLCK myosin light chain kinase |
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