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The primary structure of a triple-helical domain of collagen type VIII from bovine Descemet's membrane.

作者信息

Mann K, Jander R, Korsching E, Kühn K, Rauterberg J

机构信息

Max-Planck-Institut für Biochemie, Abt. Bindegewebsforschung, Martinsried, FRG.

出版信息

FEBS Lett. 1990 Oct 29;273(1-2):168-72. doi: 10.1016/0014-5793(90)81076-z.

Abstract

We have isolated and sequenced a fragment of 469 amino acid residues from bovine type VIII collagen. The sequence was composed of a series of Gly-X-Y repeats which was interrupted 8 times by short imperfections. The number and relative location of these interruptions were similar to those of chicken alpha 1(X) and rabbit alpha 1(VIII) chain triple-helical domains. Comparison to published N-terminal sequences to two triple-helical fragments of bovine type VIII collagen and to the cDNA derived sequence of the rabbit alpha 1(VIII) chain showed that this fragment was the triple-helical domain of a second type VIII collagen chain which we designate alpha 2(VIII).

摘要

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