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Electrophoretic investigation of muscle extracts of low ionic strength

  • Biochemistry and Biophysics
  • Published:
Bulletin of Experimental Biology and Medicine Aims and scope

Abstract

The composition of protein subunits extracted from muscle homogenates of various types by salt media of low ionic strength was studied by electrophoresis in polyacrylamide gel with sodium dodecyl sulfate. Extracts from smooth muscles contained a premyosin subunit with a molecular weight of 230,000, the heavy chain of myosin, actin, and certain other proteins. Extracts of low ionic strength from smooth muscles possessed Mg- and Ca-activated ATPase activity. A premyosin subunit also was found in extracts of low ionic strengths from homogenates of skeletal muscles. It is postulated that the premyosin subunit is a component of the enzyme system responsible for the ATPase properties of extracts of low ionic strengths from homogenates of different types of muscle.

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Authors and Affiliations

  1. Academy of Medical Sciences of the USSR, USSR

    I. I. Ivanov (Academician)

Authors
  1. N. A. Lebedeva
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  2. A. L. Solov'ev
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  3. L. F. Efimova
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  4. I. I. Ivanov
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Additional information

Leningrad Pediatric Medical Institute. S. M. Kirov Military Medical Academy, Leningrad. Translated from Byulleten' Éksperimental'noi Biologii i Meditsiny, Vol. 84, No. 12, pp. 667–669, December, 1977.

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Lebedeva, N.A., Solov'ev, A.L., Efimova, L.F. et al. Electrophoretic investigation of muscle extracts of low ionic strength. Bull Exp Biol Med 84, 1700–1703 (1977). https://doi.org/10.1007/BF00804810

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  • DOI: https://doi.org/10.1007/BF00804810

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