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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
2
|
pubmed:dateCreated |
1979-12-18
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pubmed:abstractText |
Partially degraded hyaluronate was coupled to AH-Sepharose 4B using carbodiimide. Approximately 1 mg of hyaluronate was incorporated per ml of wet gel. The derivatized gel was used to purify components of the hyaluronate-proteoglycan complex of cartilage. Two link-proteins were isolated from a crude cartilage extract by affinity binding to the gel and eluted with 4 M guanidinium chloride. By the same procedure one link-protein and the globular portion of the proteoglycan monomer were isolated from a trypsin-treated cartilage extract and were separated from each other by subsequent gel chromatography on Sepharose 6B and Sephacryl S-200. The affinity technique was also used for the preparation of these proteins labelled with dansyl groups.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
|
pubmed:chemical | |
pubmed:status |
MEDLINE
|
pubmed:month |
Jun
|
pubmed:issn |
0006-3002
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pubmed:author | |
pubmed:issnType |
Print
|
pubmed:day |
19
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pubmed:volume |
578
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
281-9
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pubmed:dateRevised |
2003-11-14
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pubmed:meshHeading |
pubmed-meshheading:486527-Animals,
pubmed-meshheading:486527-Carrier Proteins,
pubmed-meshheading:486527-Cartilage,
pubmed-meshheading:486527-Cattle,
pubmed-meshheading:486527-Chromatography, Affinity,
pubmed-meshheading:486527-Hyaluronic Acid,
pubmed-meshheading:486527-Nasal Cavity,
pubmed-meshheading:486527-Proteoglycans,
pubmed-meshheading:486527-Trypsin
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pubmed:year |
1979
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pubmed:articleTitle |
Affinity chromatography on immobilized hyaluronate and its application to the isolation of hyaluronate binding properties from cartilage.
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pubmed:publicationType |
Journal Article
|