Abstract:

Collagen was isolated from swimbladder tissue of Tachysurus maculates by acid extraction. Electrophoresis on SDS-PAGE showed that the a1 and a2 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 dimmers ß11 and ß 12 after the collagen was denatured. Thus, the native collagen molecule in this study has the formula, (a1)2 a2 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 (Ts) of the swimbladder tissue was 54.5ºC. The single peak obtained around Ts by hydrothermanl isometric tension (HIT) measurements indicated the presence of only heat-labile cross-links.

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Date 1998/09/01

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