Identification of the cartilage α 1(XI) chain in type V collagen from bovine bone

Christopher Niyibizi, David R. Eyre

Research output: Contribution to journalArticle

83 Citations (Scopus)

Abstract

Type V collagen prepared from bovine bone was resolved into three distinct α-chains by high performance liquid chromatography and gel electrophoresis. Peptide mapping established two chains as α 1(V) and α 2(V) as expected and the third as the cartilage α 1(XI) chain (previously thought to be unique to cartilage). In adult bone, the type V collagen fraction was richer in α 1(XI) chains than in fetal bone (about 1/3 of the chains in the adult). How these polypeptides are organized into native molecules is not yet clear, though the stoichiometry suggests cross-type heterotrimers between the type V and XI chains.

Original languageEnglish (US)
Pages (from-to)314-318
Number of pages5
JournalFEBS Letters
Volume242
Issue number2
DOIs
StatePublished - Jan 2 1989

Fingerprint

Collagen Type V
Cartilage
Bone
Bone and Bones
Peptides
Peptide Mapping
High performance liquid chromatography
Electrophoresis
Stoichiometry
Gels
High Pressure Liquid Chromatography
Molecules

All Science Journal Classification (ASJC) codes

  • Biophysics
  • Structural Biology
  • Biochemistry
  • Molecular Biology
  • Genetics
  • Cell Biology

Cite this

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Identification of the cartilage α 1(XI) chain in type V collagen from bovine bone. / Niyibizi, Christopher; Eyre, David R.

In: FEBS Letters, Vol. 242, No. 2, 02.01.1989, p. 314-318.

Research output: Contribution to journalArticle

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