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Volume 273, Issue 1-2 p. 168-172
Full-length article
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The primary structure of a triple-helical domain of collagen type VIII from bovine Descemet's membrane

Karlheinz Mann

Karlheinz Mann

Max-Planck-Institut für Biochemie, Abt. Bindegewebsforschung, D-8033 Martinsried, FRG

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Renate Jander

Renate Jander

Institut für Arterioskleroseforschung an der Universität Münster, D-4400 Münster, FRG

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Eberhard Korsching

Eberhard Korsching

Institut für Arterioskleroseforschung an der Universität Münster, D-4400 Münster, FRG

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Klaus Kühn

Klaus Kühn

Max-Planck-Institut für Biochemie, Abt. Bindegewebsforschung, D-8033 Martinsried, FRG

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Jürgen Rauterberg

Jürgen Rauterberg

Institut für Arterioskleroseforschung an der Universität Münster, D-4400 Münster, FRG

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First published: October 29, 1990
Citations: 25
Correspondence address: K. Mann, Max-Planck-Institut für Biochemie, Abt. Bindegewebsforschung, D-8033 Martinsried, FRG.

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 α1(X) and rabbit αl(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 αl(VIII) chain showed that this fragment was the triple-helical domain of a second type VIII collagen chain which we designate α2(VIII).