The component αchains of type V collagen from bovine bone were isolated and structurally characterized by gel electrophoresis, high performance liquid chromatography (HPLC) and amino acid sequence analysis. Three distinct αchains were identified. Two of these were the well described α1(V) and α2(V) chains; the third proved to be identical to the cartilage α1(XI) chain. In adult bone the ratio between the three chains was about 1:1:1. Native type V collagen was cleaved by trypsin at 33°C or 37°C into 3/5 fragments. Aminoterminal sequence analysis of the α1(V) and α1(XI) fragments showed they both resulted from trypsin cleavage between residue 434 and 435. Trypsin apparently cleaves the type V molecule within a relatively unstable domain of the triple helix which presumably may also be a natural site of initial cleavage by a protease in vivo.
All Science Journal Classification (ASJC) codes
- Orthopedics and Sports Medicine
- Molecular Biology
- Cell Biology