Linked Life Data

3112157

Source:http://linkedlifedata.com/resource/pubmed/id/3112157

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
23
pubmed:dateCreated
1987-9-17
pubmed:abstractText
Three collagen chains, 1 alpha, 2 alpha, and 3 alpha, have previously been identified in the cartilaginous extracellular matrix and have been referred to collectively as type XI collagen. The structure of type XI is poorly defined. Neither the organization of these collagen chains into trimeric molecules nor the extent of proteolytic processing has been adequately determined. Formaldehyde-derived covalent cross-links were introduced into the native molecules. As judged by velocity sedimentation, the cross-links formed were predominantly intramolecular and led to the formation of covalent trimeric molecules. Chromatographic analysis of trimers is most consistent with a heterotrimer (1 alpha, 2 alpha, 3 alpha) being the predominant form. To investigate the structure of type XI as it occurs in the matrix, sterna from chick embryos treated with beta-aminopropionitrile were solubilized without proteolysis with pepsin. Electrophoretic analysis revealed that all three chains of type XI retain non-triple-helical domains. Some heterogeneity was observed in the size of the 1 alpha chain. Metabolic labeling and long term chase experiments suggested that this heterogeneity in the size of 1 alpha may be due to slow or incomplete posttranslational proteolytic processing.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Aug
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
15
pubmed:volume
262
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
11345-50
pubmed:dateRevised
2008-11-21
pubmed:meshHeading
pubmed:year
1987
pubmed:articleTitle
Type XI collagen is a heterotrimer with the composition (1 alpha, 2 alpha, 3 alpha) retaining non-triple-helical domains.
pubmed:publicationType
Journal Article