TY - JOUR
T1 - Bone type v collagen
T2 - Chain composition and location of a trypsin cleavage site
AU - Niyibizi, Christopher
AU - Eyre, David R.
N1 - Funding Information:
We thank Vince Farnsworth of Porton Instruments, Inc., Tarzana, CA, for carrying out the protein sequencing. The work was supported in part by us PHS NIH grants AR37318 and AR36794.
PY - 1989
Y1 - 1989
N2 - 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.
AB - 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.
UR - http://www.scopus.com/inward/record.url?scp=0024809327&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=0024809327&partnerID=8YFLogxK
U2 - 10.3109/03008208909023894
DO - 10.3109/03008208909023894
M3 - Article
C2 - 2612158
AN - SCOPUS:0024809327
SN - 0300-8207
VL - 20
SP - 247
EP - 250
JO - Connective Tissue Research
JF - Connective Tissue Research
IS - 1-4
ER -