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rdf:type |
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lifeskim:mentions |
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pubmed:dateCreated |
1996-11-13
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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.
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/8809038-1033911,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8809038-1425603,
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http://linkedlifedata.com/resource/pubmed/commentcorrection/8809038-264696,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8809038-2764886,
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http://linkedlifedata.com/resource/pubmed/commentcorrection/8809038-2966502,
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http://linkedlifedata.com/resource/pubmed/commentcorrection/8809038-992098
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Sep
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pubmed:issn |
0264-6021
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
1
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pubmed:volume |
318 ( Pt 2)
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
497-503
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pubmed:dateRevised |
2009-11-18
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pubmed:meshHeading |
pubmed-meshheading:8809038-Amino Acid Sequence,
pubmed-meshheading:8809038-Animals,
pubmed-meshheading:8809038-Aorta,
pubmed-meshheading:8809038-Base Sequence,
pubmed-meshheading:8809038-Borohydrides,
pubmed-meshheading:8809038-Cattle,
pubmed-meshheading:8809038-Chromatography, Gel,
pubmed-meshheading:8809038-Collagen,
pubmed-meshheading:8809038-Cross-Linking Reagents,
pubmed-meshheading:8809038-Disulfides,
pubmed-meshheading:8809038-Macromolecular Substances,
pubmed-meshheading:8809038-Models, Structural,
pubmed-meshheading:8809038-Molecular Sequence Data,
pubmed-meshheading:8809038-Muscle, Smooth, Vascular,
pubmed-meshheading:8809038-Peptide Fragments,
pubmed-meshheading:8809038-Protein Structure, Secondary,
pubmed-meshheading:8809038-Trypsin
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pubmed:year |
1996
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pubmed:articleTitle |
Cross-link analysis of the C-telopeptide domain from type III collagen.
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pubmed:affiliation |
Institut für Arterioskleroseforschung, Universität Münster, Federal Republic of Germany.
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pubmed:publicationType |
Journal Article
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