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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
2
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pubmed:dateCreated |
1980-9-23
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pubmed:abstractText |
A polymeric form of the alpha 1-chain C-terminal peptide alpha 1 CB6 (poly-alpha 1 CB6) was purified from CNBr digests of insoluble bovine tendon type-I-collagen by gel filtration and ion-exchage chromatography. The purified material had a molecular weight of 1.5 x 10(6)-5 x 10(6) on gel filtration and an amino acid content virtually identical with that of monomeric peptide alpha 1 CB6. The material could be adsorbed on affinity gels containing immobilized anti-(alpha 1 CB6-peptide non-helical region) antibodies and was an inhibitor of haemagglutination by the same antibodies of alpha 1 CB6-peptide-coated sheep erythrocytes. Periodate treatment of the material had no effect. Alkali hydrolysates were shown to contain two unknown amino acids, which were purified by gel filtration and ion-exchange chromatography in volatile buffers and are believed to be components of the mature cross-link of collagen.
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/6249253-330230,
http://linkedlifedata.com/resource/pubmed/commentcorrection/6249253-33394,
http://linkedlifedata.com/resource/pubmed/commentcorrection/6249253-4354949,
http://linkedlifedata.com/resource/pubmed/commentcorrection/6249253-458854,
http://linkedlifedata.com/resource/pubmed/commentcorrection/6249253-4722452,
http://linkedlifedata.com/resource/pubmed/commentcorrection/6249253-4778266,
http://linkedlifedata.com/resource/pubmed/commentcorrection/6249253-50603,
http://linkedlifedata.com/resource/pubmed/commentcorrection/6249253-508799,
http://linkedlifedata.com/resource/pubmed/commentcorrection/6249253-5102923,
http://linkedlifedata.com/resource/pubmed/commentcorrection/6249253-5451907,
http://linkedlifedata.com/resource/pubmed/commentcorrection/6249253-5832303,
http://linkedlifedata.com/resource/pubmed/commentcorrection/6249253-761615,
http://linkedlifedata.com/resource/pubmed/commentcorrection/6249253-991856
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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 |
Feb
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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 |
185
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
373-81
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pubmed:dateRevised |
2009-11-18
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pubmed:meshHeading |
pubmed-meshheading:6249253-Amino Acids,
pubmed-meshheading:6249253-Animals,
pubmed-meshheading:6249253-Biopolymers,
pubmed-meshheading:6249253-Cattle,
pubmed-meshheading:6249253-Chemical Phenomena,
pubmed-meshheading:6249253-Chemistry,
pubmed-meshheading:6249253-Chromatography, Affinity,
pubmed-meshheading:6249253-Chromatography, Gel,
pubmed-meshheading:6249253-Chromatography, Ion Exchange,
pubmed-meshheading:6249253-Collagen,
pubmed-meshheading:6249253-Cyanogen Bromide,
pubmed-meshheading:6249253-Hemagglutination Tests,
pubmed-meshheading:6249253-Pepsin A,
pubmed-meshheading:6249253-Peptide Fragments,
pubmed-meshheading:6249253-Periodic Acid
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pubmed:year |
1980
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pubmed:articleTitle |
The chemistry of the collagen cross-links. Purification and characterization of cross-linked polymeric peptide material from mature collagen containing unknown amino acids.
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pubmed:publicationType |
Journal Article
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