Subunit composition of native myosin isoenzymes of some striated mamalian muscles

Maréchal, Georges;Biral, D.;Beckers-Bleukx, G.;Colson-Van Schoor, M.
(1989) Réunion de la Société belge de physiologie et de pharmacologie — Location: Antwerpen (2.December.1988)

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Authors
  • Maréchal, Georgesorcid-logoUCLouvain
    Author
  • Biral, D.
    Author
  • Beckers-Bleukx, G.UCLouvain
    Author
  • Colson-Van Schoor, M.
    Author
Abstract
Native myosin isoenzymes from slow, fast or mixed adult striated mammalian muscles have been isolated by electrophoresis in non-dissociating conditions. Three components (SM2, SM1 and IM) are associated with slow muscles and three (FM3, FM2 and FM1) with typical fast muscles. Mixed muscles contain the three fast components and one or two slow forms. The isoenzymes were further characterized for their subunit composition, by submitting the myosin bands to a second electrophoresis in the presence of SDS. SM1 and IM myosins are hybrid forms of myosin. The three fast forms FM3, FM2, FM1 differ by their alkali-light chain content but appear to contain two fast heavy chains (MHC2A and MHC2B).

Citations

Maréchal, G., Biral, D., Beckers-Bleukx, G., & Colson-Van Schoor, M. (1989). Subunit composition of native myosin isoenzymes of some striated mamalian muscles. Archives Internationales de Physiologie et Pharmacologie, 97(1), p14. https://hdl.handle.net/2078.5/214383 (Original work published 1989)