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  • Title: Lower vertebrate collagen. Evidence for type I-like collagen in the skin of lamprey and shark.
    Author: Kimura S, Kamimura T, Takema Y, Kubota M.
    Journal: Biochim Biophys Acta; 1981 Jul 28; 669(2):251-7. PubMed ID: 7284439.
    Abstract:
    The soluble skin collagens of the lamprey, Entosphenus japonicus, and the great blue shark, Prionace glauca, have been isolated and characterized with respect to their chain composition. Chromatography on CM-cellulose of the denatured skin collagens and agarose gel filtration, sodium dodecyl sulfate-polyacrylamide gel electrophoresis and chemical analysis of the chromatographic fractions revealed that the two distinct subunits, alpha 1 and alpha 2, were present in a molar ratio of about 2:1. Thus, the chain composition of both lower vertebrate collagens is designated by the formula (alpha 1)2 alpha 2, similar to that of Type I collagen in higher vertebrate tissues. However, electrophoresis of the collagens in sodium dodecyl sulfate showed mostly a single type of alpha component. This seems to be due to the preferential crosslinking of alpha 1 into beta 11 dimers for the lamprey collagen and of alpha 2 into beta 12 dimers for the shark protein. These composite findings indicate that Type I-like collagen is widely distributed in the skin of vertebrates ranging from cyclostomes to mammalians.
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