Tension development in skinned glycerinated rabbit psoas fiber segments irrigated with soluble myosin fragments

Julian Borejdo, Avraham Oplatka

Research output: Contribution to journalArticle

25 Citations (Scopus)

Abstract

Single glycerinated rabbit psoas muscle fibers were skinned by splitting them lengthwise. The fiber segments thus obtained were more easily accessible to solutes in the surrounding medium than the intact fibers. Using such segments, active tension could be fully abolished by adding N-ethylmaleimide under conditions which lead to inhibition of actin activation of the ATPase activity of myosin. Such muscles could, however, develop tension after irrigation with myosin or with the water-soluble active myosin fragments heavy meromyosin (HMM) or its subfragment 1 (HMM-S1). The induced tensions increased with increasing protein concentration in the irrigating solution. At any given protein concentration, the tension generated by myosin was larger than that produced by HMM which was, in turn, greater than that induced by HMM-S1 e.g. at 15 mg/ml protein the tensions produced by these three myosin moieties were 44.0, 14.0 and 2.8 g/cm2, respectively. The tension was found to be intimately associated with ATP splitting; thus, HMM and HMM-S1 which have been treated with reagents abolishing actin-activated ATPase failed to induce tension development. A contractile force may thus be generated through the interaction with actin of the water-soluble, enzymatically active, myosin subfragments involving the splitting of ATP.

Original languageEnglish
Pages (from-to)241-258
Number of pages18
JournalBBA - Bioenergetics
Volume440
Issue number1
DOIs
StatePublished - 9 Jul 1976

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Myosin Subfragments
Myosins
Rabbits
Fibers
Muscle
Actins
Adenosine Triphosphate
Psoas Muscles
Proteins
Ethylmaleimide
Water
Irrigation
Adenosine Triphosphatases
Chemical activation
Muscles

Cite this

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abstract = "Single glycerinated rabbit psoas muscle fibers were skinned by splitting them lengthwise. The fiber segments thus obtained were more easily accessible to solutes in the surrounding medium than the intact fibers. Using such segments, active tension could be fully abolished by adding N-ethylmaleimide under conditions which lead to inhibition of actin activation of the ATPase activity of myosin. Such muscles could, however, develop tension after irrigation with myosin or with the water-soluble active myosin fragments heavy meromyosin (HMM) or its subfragment 1 (HMM-S1). The induced tensions increased with increasing protein concentration in the irrigating solution. At any given protein concentration, the tension generated by myosin was larger than that produced by HMM which was, in turn, greater than that induced by HMM-S1 e.g. at 15 mg/ml protein the tensions produced by these three myosin moieties were 44.0, 14.0 and 2.8 g/cm2, respectively. The tension was found to be intimately associated with ATP splitting; thus, HMM and HMM-S1 which have been treated with reagents abolishing actin-activated ATPase failed to induce tension development. A contractile force may thus be generated through the interaction with actin of the water-soluble, enzymatically active, myosin subfragments involving the splitting of ATP.",
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Tension development in skinned glycerinated rabbit psoas fiber segments irrigated with soluble myosin fragments. / Borejdo, Julian; Oplatka, Avraham.

In: BBA - Bioenergetics, Vol. 440, No. 1, 09.07.1976, p. 241-258.

Research output: Contribution to journalArticle

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