| pubmed-article:486527 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:486527 | lifeskim:mentions | umls-concept:C0007301 | lld:lifeskim |
| pubmed-article:486527 | lifeskim:mentions | umls-concept:C0178695 | lld:lifeskim |
| pubmed-article:486527 | lifeskim:mentions | umls-concept:C0204727 | lld:lifeskim |
| pubmed-article:486527 | lifeskim:mentions | umls-concept:C0205409 | lld:lifeskim |
| pubmed-article:486527 | lifeskim:mentions | umls-concept:C1167622 | lld:lifeskim |
| pubmed-article:486527 | lifeskim:mentions | umls-concept:C0185125 | lld:lifeskim |
| pubmed-article:486527 | lifeskim:mentions | umls-concept:C0008551 | lld:lifeskim |
| pubmed-article:486527 | lifeskim:mentions | umls-concept:C0871161 | lld:lifeskim |
| pubmed-article:486527 | pubmed:issue | 2 | lld:pubmed |
| pubmed-article:486527 | pubmed:dateCreated | 1979-12-18 | lld:pubmed |
| pubmed-article:486527 | 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. | lld:pubmed |
| pubmed-article:486527 | pubmed:language | eng | lld:pubmed |
| pubmed-article:486527 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:486527 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:486527 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:486527 | pubmed:month | Jun | lld:pubmed |
| pubmed-article:486527 | pubmed:issn | 0006-3002 | lld:pubmed |
| pubmed-article:486527 | pubmed:author | pubmed-author:TengbladAA | lld:pubmed |
| pubmed-article:486527 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:486527 | pubmed:day | 19 | lld:pubmed |
| pubmed-article:486527 | pubmed:volume | 578 | lld:pubmed |
| pubmed-article:486527 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:486527 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:486527 | pubmed:pagination | 281-9 | lld:pubmed |
| pubmed-article:486527 | pubmed:dateRevised | 2003-11-14 | lld:pubmed |
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| pubmed-article:486527 | pubmed:meshHeading | pubmed-meshheading:486527-P... | lld:pubmed |
| pubmed-article:486527 | pubmed:year | 1979 | lld:pubmed |
| pubmed-article:486527 | pubmed:articleTitle | Affinity chromatography on immobilized hyaluronate and its application to the isolation of hyaluronate binding properties from cartilage. | lld:pubmed |
| pubmed-article:486527 | pubmed:publicationType | Journal Article | lld:pubmed |
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