Abstract
Pepsin-solubilized collagens prepared from the muscle tissues (ordinary and dark muscles) of Japanese amberjack were separated into two fractions, major and minor, by ammonium sulphate precipitation. Collagens in these fractions were further purified by cation-exchange column chromatography. The results of SDS-PAGE, peptide mapping, and amino acid analysis suggested that the purified major and minor collagens might be classified as type I and V collagens, respectively. Each type of collagen was fundamentally similar, among the ordinary and dark muscles, in amino acid compositions and peptide maps.
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