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Procedures have been developed for the preparation of pure myosin heavy chain (h-myosin) by preparative gel electrophoresis, and for the characterization of h-myosin by cyanogen bromide peptide mapping. Major sources of error are the oxidation of methionine and the proteolytic splitting of the chain during purification. These errors have been eliminated. A peculiar feature is the doubling or quadrupling of a peptide of molecular weight 17 000. The results show structural differences between isomyosins derived from myonal types within the same animal, as well as interspecies differences.
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