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Identification of the cartilage α 1(XI) chain in type V collagen from bovine bone
Author(s) -
Niyibizi Christopher,
Eyre David R.
Publication year - 1989
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(89)80492-2
Subject(s) - cartilage , collagen, type i, alpha 1 , chemistry , alpha (finance) , type i collagen , gel electrophoresis , type ii collagen , peptide , chain (unit) , biochemistry , anatomy , biology , endocrinology , extracellular matrix , medicine , physics , construct validity , nursing , astronomy , patient satisfaction
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.