Actin-Heavy Meromyosin Binding. Determination of Binding Stoichiometry from Adenosine Triphosphatase Kinetic Measurements

A. A. Rizzino, W. W. Barouch, E. Eisenberg, C. Moos

Research output: Contribution to journalArticle

46 Scopus citations

Abstract

Enzyme kinetic measurements of the effects of actin on the heavy meromyosin adenosine triphosphatase (ATPase) are used for a study of the binding of heavy meromyosin to actin. In the absence of free magnesium ions, the potassium-activated ATPase of heavy meromyosin is inhibited by actin, and this inhibition is used as a quantitative measuee of binding. The activation of the heavy meromyosin ATPase by actin in the presence of magnesium ions is also used as a measure of binding. Both kinds of data, when analyzed according to the theory of multiple equilibria, give simple binding curves with a binding stoichiometry of 1 mole of heavy meromyosin/mole of monomsrs in F-actin.

Original languageEnglish (US)
Pages (from-to)2402-2408
Number of pages7
JournalBiochemistry
Volume9
Issue number12
DOIs
Publication statusPublished - Jun 1 1970

    Fingerprint

ASJC Scopus subject areas

  • Biochemistry

Cite this