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. 1972 Apr;127(2):419–424. doi: 10.1042/bj1270419

The enzymic properties of a modified ox heart myosin adenosine triphosphatase on covalent binding to an insoluble cellulose matrix

Phyllis Liu-Osheroff 1, Richard John Guillory 1,*
PMCID: PMC1178602  PMID: 4263190

Abstract

The preparation of ox heart myosin and its partial digestion with cellulose-bound papain is described. A procedure is outlined by which heavy meromyosin subfragment 1 can be covalently bound to a cellulose ion-exchange matrix. Attachment of heavy meromyosin subfragment 1 to the insoluble matrix results in a change in the ion specificity towards ATP hydrolysis. Unlike the soluble enzyme the bound form is activated by both Ca2+ and Mg2+. Maximal activation by Ca2+ occurred at a lower concentration for the bound enzyme. Mg2+ activates at a concentration which causes near-maximal inhibition of the Ca2+-activated adenosine triphosphatase (ATPase) of the non-bound enzyme. The Mg2+-activated ATPase of the bound enzyme was in turn inhibited by the presence of Ca2+. The activation by Mg2+ resembles the characteristic enzymic action of the actin-subfragment 1 complex.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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