SEPARATION OF MYOSIN HEAVY CHAIN ISOFORMS IN RAT SKELETAL MUSCLES BY GRADIENT SODIUM DODECYL SULFATE-POLYACRYLAMIDE GEL ELECTROPHORESIS

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Abstract
This study was conducted to investigate the electrophoretic condition for the separation of a novel myosin heavy chain isoform, designated as HCIId, in rat skeletal muscles by gradient sodium dodecyl sulfate-polyacrylamide gel electrophoresis. HCIId was separated on a polyacrylamide (5-8%)/glycerol (30-40%) gradient gel when electrophoresis was performed at 150 V for about 18 h at 8.degree. C. HCIId was observed in most fast-twitch muscles. Of those muscles, the deep portion of the masseter muscle contained the most abundant HCIId and one of the masseter muscles contained the neonatal-type MHC.