Enhanced protein electrophoresis technique for separating human skeletal muscle myosin heavy chain isoforms

Academic Article

Abstract

  • Talmadge and Roy (J. Appl. Physiol. 1993, 75, 2337-2340) previously established a sodium dodecyl sulfate - polyacrylamide gel electrophoresis (SDS-PAGE) protocol for separating all four rat skeletal muscle myosin heavy chain (MHC) isoforms (MHC I, IIa, IIx, IIb); however, when applied to human muscle, the type II MHC isoforms (IIa, IIx) are not clearly distinguished. In this brief paper we describe a modification of the SDS-PAGE protocol which yields distinct and consistent separation of all three adult human MHC isoforms (MHC I, IIa, IIx) in a minigel system. MHC specificity of each band was confirmed by Western blot using three monoclonal IgG antibodies (mAbs) immunoreactive against MHCl (mAb MHCs, Novacastra Laboratories), MHCl+IIa (mAb BF-35), and MHClIa+IIx (mAb SC-71). Results provide a valuable SDS-PAGE minigel technique for separating MHC isoforms in human muscle without the difficult task of casting gradient gels.
  • Authors

    Published In

  • ELECTROPHORESIS  Journal
  • Pubmed Id

  • 9114993
  • Author List

  • Bamman MM; Clarke MSF; Talmadge RJ; Feeback DL
  • Start Page

  • 466
  • End Page

  • 468
  • Volume

  • 20
  • Issue

  • 3