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The primary structure of a triple‐helical domain of collagen type VIII from bovine Descemet's membrane
Author(s) -
Mann Karlheinz,
Jander Renate,
Korsching Eberhard,
Kühn Klaus,
Rauterberg Jürgen
Publication year - 1990
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(90)81076-z
Subject(s) - triple helix , chemistry , protein primary structure , sequence (biology) , peptide sequence , microbiology and biotechnology , domain (mathematical analysis) , stereochemistry , biology , biochemistry , gene , mathematics , mathematical analysis
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).