• 1 January 1975
    • journal article
    • research article
    • Vol. 17  (10) , 1148-+
Abstract
The protein subunit composition of isolated myofibrils of rabbit skeletal muscle is studied by polyacrylamide gel disc-electrophoresis in the presence of sodium dodecyl sulfate (SDS), and the method is described in detail. The electrophoretic patterns of SDS-solubilized myofibrils obtained by disc-SDS-electrophoresis and by SDS-electrophoresis in continuous buffer system according to Weber and Osborn are compared. The former results in a markedly improved resolution and discloses some additional protein components; the origin of these additional components is discussed. A standard curve is given for determination of polypeptide chain molecular weights by disc-SDS-electrophoresis.

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