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pubmed-article:2612158pubmed:abstractTextThe 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.lld:pubmed
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pubmed-article:2612158pubmed:authorpubmed-author:NiyibiziCClld:pubmed
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pubmed-article:2612158pubmed:volume20lld:pubmed
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pubmed-article:2612158pubmed:pagination247-50lld:pubmed
pubmed-article:2612158pubmed:dateRevised2007-11-14lld:pubmed
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pubmed-article:2612158pubmed:year1989lld:pubmed
pubmed-article:2612158pubmed:articleTitleBone type V collagen: chain composition and location of a trypsin cleavage site.lld:pubmed
pubmed-article:2612158pubmed:affiliationDepartment of Orthopaedics, University of Washington, Seattle.lld:pubmed
pubmed-article:2612158pubmed:publicationTypeJournal Articlelld:pubmed
pubmed-article:2612158pubmed:publicationTypeResearch Support, U.S. Gov't, P.H.S.lld:pubmed
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