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

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

Research output: Contribution to journalArticle

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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
StatePublished - Jun 1 1970

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Myosin Subfragments
Enzyme kinetics
Stoichiometry
Adenosine Triphosphatases
Actins
Magnesium
Ions
Potassium
Chemical activation
Enzymes

ASJC Scopus subject areas

  • Biochemistry

Cite this

Actin-Heavy Meromyosin Binding. Determination of Binding Stoichiometry from Adenosine Triphosphatase Kinetic Measurements. / Rizzino, A Angie; Barouch, W. W.; Eisenberg, E.; Moos, C.

In: Biochemistry, Vol. 9, No. 12, 01.06.1970, p. 2402-2408.

Research output: Contribution to journalArticle

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