Linked Life Data

2612158

Source:http://linkedlifedata.com/resource/pubmed/id/2612158

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1-4
pubmed:dateCreated
1990-3-7
pubmed:abstractText
The component alpha-chains 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 alpha-chains were identified. Two of these were the well described alpha 1 (V) and alpha 2 (V) chains; the third proved to be identical to the cartilage alpha 1 (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 degrees C or 37 degrees C into 3/5 fragments. Aminoterminal sequence analysis of the alpha 1 (V) and alpha 1 (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.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:issn
0300-8207
pubmed:author
pubmed:issnType
Print
pubmed:volume
20
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
247-50
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed:year
1989
pubmed:articleTitle
Bone type V collagen: chain composition and location of a trypsin cleavage site.
pubmed:affiliation
Department of Orthopaedics, University of Washington, Seattle.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S.