Binding Of Heavy Meromyosin And Subfragment-1 To Thin Filaments In Myofibrils And Single Muscle Fibers

Julian Borejdo, Olga Assulin

Research output: Contribution to journalArticle

14 Citations (Scopus)

Abstract

The binding of fluorescently labeled heavy meromyosin (HMM) and heavy meromyosin subfragment-1 (S-l) to thin filaments of myofibrils and of rabbit psoas muscle fibers was measured under conditions of rigor and contraction. The fragments diffused rapidly into the myofibrillar space and bound specifically to the thin filaments. The fragments bound strongest and in a uniform fashion to myofibrils in which the competition from indigenous myosin was abolished by removing it with Hasselbach-Schneider solution. Under these conditions, the rigor Kavalues for HMM and S-l were 1.5 X 106M-1and 4.8 x 104M-1, respectively. The stoichiometry of binding was measured by independently estimating the concentration of actin sites. S-l was found to be capable of saturating all available actin sites in a myofibril or a fiber, but HMM could only occupy 50% of the sites.

Original languageEnglish
Pages (from-to)4913-4921
Number of pages9
JournalBiochemistry
Volume19
Issue number21
DOIs
StatePublished - 1 Feb 1980

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Myosin Subfragments
Myofibrils
Muscle
Muscles
Fibers
Actins
Psoas Muscles
Myosins
Stoichiometry
Rabbits

Cite this

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title = "Binding Of Heavy Meromyosin And Subfragment-1 To Thin Filaments In Myofibrils And Single Muscle Fibers",
abstract = "The binding of fluorescently labeled heavy meromyosin (HMM) and heavy meromyosin subfragment-1 (S-l) to thin filaments of myofibrils and of rabbit psoas muscle fibers was measured under conditions of rigor and contraction. The fragments diffused rapidly into the myofibrillar space and bound specifically to the thin filaments. The fragments bound strongest and in a uniform fashion to myofibrils in which the competition from indigenous myosin was abolished by removing it with Hasselbach-Schneider solution. Under these conditions, the rigor Kavalues for HMM and S-l were 1.5 X 106M-1and 4.8 x 104M-1, respectively. The stoichiometry of binding was measured by independently estimating the concentration of actin sites. S-l was found to be capable of saturating all available actin sites in a myofibril or a fiber, but HMM could only occupy 50{\%} of the sites.",
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Binding Of Heavy Meromyosin And Subfragment-1 To Thin Filaments In Myofibrils And Single Muscle Fibers. / Borejdo, Julian; Assulin, Olga.

In: Biochemistry, Vol. 19, No. 21, 01.02.1980, p. 4913-4921.

Research output: Contribution to journalArticle

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