| Abstract: | The protein subunit composition of isolated myofibrils of rabbit skeletal muscle is studied by polyacrylamide gel disc-electrophoresis in the presense of sodium dodecyl sulfate (SDS). The method of disc-SDS-electrophoresis 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 allows to discover some additional protein components, the origin of these additional components being discussed. A standard curve is given for determination of polypeptide chain molecular weights by disc-SDS-electrophoresis. |
