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A Protein Factor Inhibiting the Magnesium-activated Adenosine Triphosphatase of Desensitized Actomyosin

Overview
Journal Biochem J
Specialty Biochemistry
Date 1967 Sep 1
PMID 4227823
Citations 17
Authors
D J Hartshorne
S V PERRY
M C Schaub
Affiliations
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Abstract

1. The preparation and properties of a myofibrillar protein factor which inhibits the Mg(2+)-activated adenosine triphosphatase of desensitized actomyosin is described. 2. This factor had negligible effect on the Mg(2+)-activated adenosine triphosphatase of natural actomyosin and on the Ca(2+)-activated adenosine triphosphatases of desensitized actomyosin and myosin. 3. The Mg(2+)-activated inosine triphosphatase activity of desensitized actomyosin was not affected by the factor. 4. The inhibitory effect was sensitive to ionic strength. In addition to their ionic effects Mg(2+) and Ca(2+) appeared to have a specific action in reducing the effect of the inhibitor. 5. F-actin reduced the inhibition whereas Bailey-type tropo-myosin had little effect. 6. As far as can be judged from the reported experiments this factor is different from any of the previously described myofibrillar components.

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References
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PERRY S, Cotterill J . The action of thiol inhibitors on the interaction of F-actin and heavy meromyosin. Biochem J. 1964; 92(3):603-8. PMC: 1206109. DOI: 10.1042/bj0920603. View
2.
Barron S, Eisenberg E, Moos C . Actin-myosin interaction: inhibition of the myosin adenosine triphosphatase by actin. Science. 1966; 151(3717):1541-2. DOI: 10.1126/science.151.3717.1541. View
3.
Mueller H . Effect of Bailey's tropomyosin purification on EGTA-sensitizing activity. Nature. 1966; 209(5028):1128-9. DOI: 10.1038/2091128a0. View
4.
Maruyama K . Effect of actinins on the adenosinetriphosphatase activity of actomyosin at low ionic strength. J Biochem. 1966; 59(4):422-4. DOI: 10.1093/oxfordjournals.jbchem.a128319. View
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Hartshorne D, PERRY S, Davies V . A factor inhibiting the adenosine triphosphatase activity and the superprecipitation of actomyosin. Nature. 1966; 209(5030):1352-3. DOI: 10.1038/2091352a0. View