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Characterization of Collagen from the Swimbladder of Catfish (Tachysurus maculatus)

Collagen was isolated from swimbladder tissue of Tachysurus maculatus by acid extraction. Electrophoresis on SOS-PAGE showed that the a1 and '¼ chains are present in the molar ratio of 2:1. Chromatography on CM-cellulose, in addition to confirming the chain composition, showed the presence of reduced amounts of the crosslinked dimers 011 and 012 after the collagen was denatured. Thus, the native collagen molecule in this study has the formula, (a1)2a2 and corresponds to a Type I collagen. Molecular sieve chromatography gave an elution profile similar to rat tail tendon (RTT) collagen. Amino acid composition showed a higher content of Met and lower content of OH-Pro than mammalian collagen. The shrinkage temperature (T,) of the swimbladder tissue was 54.6°C. The single peak obtained around T1 by hydrothermal isometric tension (HIT) measurements indicated the presence of only heat-labile cross-links.