PREPARATION AND CHARACTERIZATION OF PEPSIN-SOLUBILIZED TYPE I COLLAGEN FROM THE SCALES OF SNAKEHEAD (OPHIOCEPHALUS ARGUS)

Pepsin-solubilized collagen prepared from the scales of snakehead (Ophiocephalus argus) was separated into two fractions, major and minor, by NaCl precipitation. The results of sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE), amino acid composition, and secondary structure showed that the major collagen was typical type I collagen; in contrast, the minor collagen might be classified as type V collagen from the SDS-PAGE patterns and precipitation properties by NaCl. A sharp decrease in solubility of type I collagen was observed at the NaCl concentration of 40 g/L. The maximum and the minimum solubilities of collagen were observed at pH 3 and 8, respectively. Peptide maps of type I collagen digested by trypsin and V8 protease were different from those of calfskin and fish skin collagens. The imino acid content of type I collagen was lower than those of mammalian collagens and so did its denaturation temperature that was 30.3C obtained by viscosity measurement.