Electrophoretic separation of bovine muscle myosin heavy chain isoforms.

This study concerns the definition of the optimum conditions for separation of adult and developmental myosin heavy chain (MHC) isoforms in bovine muscle. The various techniques published do not result in good separation of the MHC in this species. The trials carried out concerned the concentration of acrylamide and N, N'-methylene-bis-acrylamide, and more particularly the concentration of Tris in the separating gel. The finding was that analysis of adult isoforms and developmental isoforms require different conditions. A acrylamide gradient of 3.5-10% with 200 mM Tris pH 8.8 gives good resolution for adult isoforms. Under these conditions 3 fast adult isoforms are revealed. However, study of MHC isoforms throughout foetal life in bovines is complex, and requires the combined use of more than one gel (gradient 3.5-10% at 200 mM Tris and gradient 3.5-10% at 250 mM Tris).