Characterization of β-actinin: A suppressor of the elongation at the pointed end of thin filaments in skeletal muscle

Takashi Funatsu, Shin'ichi Ishiwata

    Research output: Contribution to journalArticle

    9 Citations (Scopus)

    Abstract

    We examined the physico-chemical properties and the functions of β-actinin by using a β-actinin preparation having the same properties as those reported by Maruyama et al. (J. Biochem. 81, 215-232, 1977). β-Actinin was composed of two components with molecular weights (estimated by sodium dodecyl sulfate (SDS) polyacrylamide gel electrophoresis) of 35,000 and 31,000 daltons. Their isoelectric points in 8 M urea were, respectively, 5.9 and 5.4, clearly distinguishable from those of tropomyosin, troponin T and some enzymes having similar molecular weights. β-Actinin suppressed the polymerization of actin onto the free end, i.e., the pointed end, of thin filaments in an I-Z-I brush prepared by dissolving thick filaments of a myofibril at high ionic strength. Further, β-actinin suppressed the association of actin to the whole region of an I-Z-I brush. The present study indicates that β-actinin is composed of two components and functions as a suppressor of elongation at the pointed end of thin filaments, supporting the conclusions of Maruyama et al. (J. Biochem. 81, 215-232, 1977).

    Original languageEnglish
    Pages (from-to)535-544
    Number of pages10
    JournalJournal of Biochemistry
    Volume98
    Issue number2
    Publication statusPublished - 1985 Aug

    Fingerprint

    Actinin
    Skeletal muscle
    Brushes
    Filament
    Elongation
    Muscle
    Skeletal Muscle
    Actin
    Molecular weight
    Sodium dodecyl sulfate
    Polyacrylates
    Ionic strength
    Electrophoresis
    Urea
    Chemical properties
    Gels
    Enzymes
    Polymerization
    Association reactions
    Sodium

    ASJC Scopus subject areas

    • Statistics, Probability and Uncertainty
    • Applied Mathematics
    • Physiology (medical)
    • Radiology Nuclear Medicine and imaging
    • Molecular Biology
    • Biochemistry

    Cite this

    Characterization of β-actinin : A suppressor of the elongation at the pointed end of thin filaments in skeletal muscle. / Funatsu, Takashi; Ishiwata, Shin'ichi.

    In: Journal of Biochemistry, Vol. 98, No. 2, 08.1985, p. 535-544.

    Research output: Contribution to journalArticle

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