| pubmed-article:8809038 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:8809038 | lifeskim:mentions | umls-concept:C0009332 | lld:lifeskim |
| pubmed-article:8809038 | lifeskim:mentions | umls-concept:C1514562 | lld:lifeskim |
| pubmed-article:8809038 | lifeskim:mentions | umls-concept:C1883221 | lld:lifeskim |
| pubmed-article:8809038 | lifeskim:mentions | umls-concept:C0936012 | lld:lifeskim |
| pubmed-article:8809038 | lifeskim:mentions | umls-concept:C0631180 | lld:lifeskim |
| pubmed-article:8809038 | lifeskim:mentions | umls-concept:C1883204 | lld:lifeskim |
| pubmed-article:8809038 | lifeskim:mentions | umls-concept:C1880389 | lld:lifeskim |
| pubmed-article:8809038 | pubmed:dateCreated | 1996-11-13 | lld:pubmed |
| pubmed-article:8809038 | pubmed:abstractText | Several peptides were isolated from tryptic digests of insoluble calf aorta matrix by chromatography. Reductive pyridylethylation of a tryptic 15 kDa pool released fragments deriving from the C-terminus of type III collagen. A 50-residue peptide Tc(III) was shown by sequence analysis to be the C-terminal peptide from the alpha 1(III)-chain, containing a helical and non-helical region of equal sizes. The peptide was further digested with collagenase to give Colc(III), comprising the complete C-terminal non-helical region of alpha 1(III) including a hydroxylysine in position 16c. The peptide Tc(III) x TN(III) was isolated, demonstrating covalent cross-linking between the C-terminal non-helical region of one type III molecule and the N-terminal helical cross-linking region of another. Its digestion with cyanogen bromide yielded the small fragments alpha 1(III)CB3B* and alpha 1(III)CB3C, confirming TN(III) as an N-terminal helical crosslink site. Sequence analysis of both Tc(III) x TN(III) and its collagenase-derived cross-linked peptide Colc(III) x TN(III) established the 4D-staggered alignment of adjacent collagen III molecules. The cross-link structure of both peptides was mainly dihydroxylysinonorleucine with a small amount of hydroxylysinonorleucine, indicating that the lysine residues involved in formation of the cross-links are both hydroxylated. No pyridinoline or histidinohydroxylysinonorleucine cross-links were found within the non-reduced C-telopeptide region of type III collagen. | lld:pubmed |
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| pubmed-article:8809038 | pubmed:language | eng | lld:pubmed |
| pubmed-article:8809038 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8809038 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:8809038 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:8809038 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:8809038 | pubmed:month | Sep | lld:pubmed |
| pubmed-article:8809038 | pubmed:issn | 0264-6021 | lld:pubmed |
| pubmed-article:8809038 | pubmed:author | pubmed-author:HenkelWW | lld:pubmed |
| pubmed-article:8809038 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:8809038 | pubmed:day | 1 | lld:pubmed |
| pubmed-article:8809038 | pubmed:volume | 318 ( Pt 2) | lld:pubmed |
| pubmed-article:8809038 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:8809038 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:8809038 | pubmed:pagination | 497-503 | lld:pubmed |
| pubmed-article:8809038 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
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| pubmed-article:8809038 | pubmed:year | 1996 | lld:pubmed |
| pubmed-article:8809038 | pubmed:articleTitle | Cross-link analysis of the C-telopeptide domain from type III collagen. | lld:pubmed |
| pubmed-article:8809038 | pubmed:affiliation | Institut für Arterioskleroseforschung, Universität Münster, Federal Republic of Germany. | lld:pubmed |
| pubmed-article:8809038 | pubmed:publicationType | Journal Article | lld:pubmed |
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