pubmed-article:2612158 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:2612158 | lifeskim:mentions | umls-concept:C0262950 | lld:lifeskim |
pubmed-article:2612158 | lifeskim:mentions | umls-concept:C0009335 | lld:lifeskim |
pubmed-article:2612158 | lifeskim:mentions | umls-concept:C0205145 | lld:lifeskim |
pubmed-article:2612158 | lifeskim:mentions | umls-concept:C0450429 | lld:lifeskim |
pubmed-article:2612158 | lifeskim:mentions | umls-concept:C1330957 | lld:lifeskim |
pubmed-article:2612158 | lifeskim:mentions | umls-concept:C0041236 | lld:lifeskim |
pubmed-article:2612158 | lifeskim:mentions | umls-concept:C1524075 | lld:lifeskim |
pubmed-article:2612158 | lifeskim:mentions | umls-concept:C0486616 | lld:lifeskim |
pubmed-article:2612158 | lifeskim:mentions | umls-concept:C0596311 | lld:lifeskim |
pubmed-article:2612158 | lifeskim:mentions | umls-concept:C0337112 | lld:lifeskim |
pubmed-article:2612158 | pubmed:issue | 1-4 | lld:pubmed |
pubmed-article:2612158 | pubmed:dateCreated | 1990-3-7 | lld:pubmed |
pubmed-article:2612158 | 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. | lld:pubmed |
pubmed-article:2612158 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:2612158 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:2612158 | pubmed:language | eng | lld:pubmed |
pubmed-article:2612158 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:2612158 | pubmed:citationSubset | IM | lld:pubmed |
pubmed-article:2612158 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:2612158 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:2612158 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:2612158 | pubmed:issn | 0300-8207 | lld:pubmed |
pubmed-article:2612158 | pubmed:author | pubmed-author:FAGGC GCG | lld:pubmed |
pubmed-article:2612158 | pubmed:author | pubmed-author:NiyibiziCC | lld:pubmed |
pubmed-article:2612158 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:2612158 | pubmed:volume | 20 | lld:pubmed |
pubmed-article:2612158 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:2612158 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:2612158 | pubmed:pagination | 247-50 | lld:pubmed |
pubmed-article:2612158 | pubmed:dateRevised | 2007-11-14 | lld:pubmed |
pubmed-article:2612158 | pubmed:meshHeading | pubmed-meshheading:2612158-... | lld:pubmed |
pubmed-article:2612158 | pubmed:meshHeading | pubmed-meshheading:2612158-... | lld:pubmed |
pubmed-article:2612158 | pubmed:meshHeading | pubmed-meshheading:2612158-... | lld:pubmed |
pubmed-article:2612158 | pubmed:meshHeading | pubmed-meshheading:2612158-... | lld:pubmed |
pubmed-article:2612158 | pubmed:meshHeading | pubmed-meshheading:2612158-... | lld:pubmed |
pubmed-article:2612158 | pubmed:meshHeading | pubmed-meshheading:2612158-... | lld:pubmed |
pubmed-article:2612158 | pubmed:meshHeading | pubmed-meshheading:2612158-... | lld:pubmed |
pubmed-article:2612158 | pubmed:meshHeading | pubmed-meshheading:2612158-... | lld:pubmed |
pubmed-article:2612158 | pubmed:year | 1989 | lld:pubmed |
pubmed-article:2612158 | pubmed:articleTitle | Bone type V collagen: chain composition and location of a trypsin cleavage site. | lld:pubmed |
pubmed-article:2612158 | pubmed:affiliation | Department of Orthopaedics, University of Washington, Seattle. | lld:pubmed |
pubmed-article:2612158 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:2612158 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:2612158 | lld:pubmed |