Characterization of β-Actinin: A Suppressor of the Elongation at the Pointed End of Thin Filaments in Skeletal Muscle1

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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).