| pubmed-article:1703408 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:1703408 | lifeskim:mentions | umls-concept:C0007603 | lld:lifeskim |
| pubmed-article:1703408 | lifeskim:mentions | umls-concept:C1882726 | lld:lifeskim |
| pubmed-article:1703408 | lifeskim:mentions | umls-concept:C1510827 | lld:lifeskim |
| pubmed-article:1703408 | lifeskim:mentions | umls-concept:C1998793 | lld:lifeskim |
| pubmed-article:1703408 | pubmed:dateCreated | 1991-2-27 | lld:pubmed |
| pubmed-article:1703408 | pubmed:abstractText | Rat liver plasma membranes were separated from other cellular membranes by affinity partitioning in an aqueous polymer two-phase system by using the lectin wheat-germ agglutinin covalently bound to dextran as the affinity ligand. In borate buffer the bulk of membranes partitioned in the poly(ethylene glycol)-rich top phase, whereas plasma membranes were pulled selectively into the dextran-rich bottom phase in the presence of ligand. The purity and yield of plasma membranes prepared by lectin affinity partitioning and by conventional sucrose-density-gradient centrifugation was similar, as judged from marker-enzyme activities. The affinity procedure, not dependent on lengthy centrifugations, is fast and gentle and will be advantageous when studying labile components. | lld:pubmed |
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| pubmed-article:1703408 | pubmed:language | eng | lld:pubmed |
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| pubmed-article:1703408 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:1703408 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:1703408 | pubmed:month | Jan | lld:pubmed |
| pubmed-article:1703408 | pubmed:issn | 0264-6021 | lld:pubmed |
| pubmed-article:1703408 | pubmed:author | pubmed-author:JohanssonBB | lld:pubmed |
| pubmed-article:1703408 | pubmed:author | pubmed-author:PerssonAA | lld:pubmed |
| pubmed-article:1703408 | pubmed:author | pubmed-author:JergilBB | lld:pubmed |
| pubmed-article:1703408 | pubmed:author | pubmed-author:OlssonHH | lld:pubmed |
| pubmed-article:1703408 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:1703408 | pubmed:day | 1 | lld:pubmed |
| pubmed-article:1703408 | pubmed:volume | 273(Pt 1) | lld:pubmed |
| pubmed-article:1703408 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:1703408 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:1703408 | pubmed:pagination | 173-7 | lld:pubmed |
| pubmed-article:1703408 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
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| pubmed-article:1703408 | pubmed:meshHeading | pubmed-meshheading:1703408-... | lld:pubmed |
| pubmed-article:1703408 | pubmed:year | 1991 | lld:pubmed |
| pubmed-article:1703408 | pubmed:articleTitle | Purification of rat liver plasma membranes by wheat-germ-agglutinin affinity partitioning. | lld:pubmed |
| pubmed-article:1703408 | pubmed:affiliation | Biochemistry, Chemical Centre, Lund, Sweden. | lld:pubmed |
| pubmed-article:1703408 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:1703408 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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