Characterization of an .ALPHA.3 chain from carp skin type I collagen.

DOI JASI Web Site 5 Citations
  • Miyauchi Yoshirou
    Laboratory of Biochemistry, Food Science and Technology, Tokyo University of Fisheries
  • Kimura Shigeru
    Laboratory of Biochemistry, Food Science and Technology, Tokyo University of Fisheries

Bibliographic Information

Other Title
  • コイ真皮Ｉ型コラーゲンのα３鎖の性状
  • コイ シンピ 1ガタ コラーゲン ノ アルファ 3 サ ノ セイジョウ

Search this article

Abstract

Many of teleosts are known to have Type I collagen with subunit structure of α1α2α3. Carp, however, is exceptional in that an α3 chain is absent from the swim bladder Type I collagen, but is present as a minor subunit in the skin Type I collagen. In this study, the skin α3 chain of carp was isolated by CM-cellulose chromatography in combination with Sepharose CL-4B gel filtration and was characterized with respect to its amino acid composi-tion and peptide map. α3 was found to be genetically distinct from αl and α2 and is as-sumed to exist as an αlα2α3 heterotrimer. Moreover, α3 was intermediate in chemical nature between αl and α2, but showed more similarities to αl than to α2. These results suggest that the skin α3 chain diverged from its al chain.

Journal

  • NIPPON SUISAN GAKKAISHI

    NIPPON SUISAN GAKKAISHI 56 (9), 1509-1514, 1990

    The Japanese Society of Fisheries Science

Citations (5)*help

See more

Keywords

Details 詳細情報について

Report a problem

Back to top