The primary structure of a triple-helical domain of collagen type VIII from bovine Descemet's membrane.
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).
Mann
K
K
Max-Planck-Institut für Biochemie, Abt. Bindegewebsforschung, Martinsried, FRG.
Jander
R
R
Korsching
E
E
Kühn
K
K
Rauterberg
J
J
D000595:Amino Acid Sequence; D000818:Animals; D002417:Cattle; D002850:Chromatography, Gel; D002851:Chromatography, High Pressure Liquid; D003094:Collagen / Q000737:chemistry* / Q000302:isolation & purification; D003886:Descemet Membrane / Q000737:chemistry*; D008969:Molecular Sequence Data; D010446:Peptide Fragments / Q000302:isolation & purification; D011487:Protein Conformation; D012689:Sequence Homology, Nucleic Acid
D010446:Peptide Fragments; D003094:Collagen