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

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).

Publication types

  • Comparative Study

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Cattle
  • Chromatography, Gel
  • Chromatography, High Pressure Liquid
  • Collagen / chemistry*
  • Collagen / isolation & purification
  • Descemet Membrane / chemistry*
  • Molecular Sequence Data
  • Peptide Fragments / isolation & purification
  • Protein Conformation
  • Sequence Homology, Nucleic Acid

Substances

  • Peptide Fragments
  • Collagen