| pubmed-article:7710065 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:7710065 | lifeskim:mentions | umls-concept:C0033684 | lld:lifeskim |
| pubmed-article:7710065 | lifeskim:mentions | umls-concept:C0596607 | lld:lifeskim |
| pubmed-article:7710065 | lifeskim:mentions | umls-concept:C1998793 | lld:lifeskim |
| pubmed-article:7710065 | lifeskim:mentions | umls-concept:C0205349 | lld:lifeskim |
| pubmed-article:7710065 | lifeskim:mentions | umls-concept:C0146953 | lld:lifeskim |
| pubmed-article:7710065 | pubmed:issue | 1 | lld:pubmed |
| pubmed-article:7710065 | pubmed:dateCreated | 1995-5-10 | lld:pubmed |
| pubmed-article:7710065 | pubmed:abstractText | Triton X-114 phase partitioning has frequently been used to obtain preparations enriched in glycosylphosphatidylinositol (GPI)-anchored proteins and other hydrophobic proteins from crude cellular homogenates. We have developed a new modification of this phase-partitioning technique which allows two distinct GPI-anchored proteins of Tetrahymena mimbres to be separated from other hydrophobic as well as hydrophilic proteins and recovered in approximately 90% yield. The unique feature of the new method is a 24-h incubation of the first Triton X-114 extract at -20 degrees C. This improves the partitioning of GPI-anchored proteins into the detergent phase while promoting the aggregation of other hydrophobic proteins. Individual GPI-anchored proteins in the detergent phase are then purified to near homogeneity by one-step preparative sodium dodecyl sulfate (SDS)-polyacrylamide gel electrophoresis. By substituting Triton X-114/water mixtures for the conventional SDS buffer used to collect proteins eluting from the preparative gel, the purified GPI-anchored protein can be rapidly concentrated from relatively large volumes of eluate by phase partitioning at 32 degrees C. The method is also effective in separating mammalian GPI-anchored alkaline phosphatase from other proteins. It is likely to be of general utility in characterizing the GPI anchor structures associated with nonabundant and abundant GPI-anchored proteins coexisting within the same cell type. | lld:pubmed |
| pubmed-article:7710065 | pubmed:language | eng | lld:pubmed |
| pubmed-article:7710065 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7710065 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:7710065 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7710065 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7710065 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7710065 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7710065 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:7710065 | pubmed:month | Jan | lld:pubmed |
| pubmed-article:7710065 | pubmed:issn | 0003-2697 | lld:pubmed |
| pubmed-article:7710065 | pubmed:author | pubmed-author:ThompsonG... | lld:pubmed |
| pubmed-article:7710065 | pubmed:author | pubmed-author:OhY DYD | lld:pubmed |
| pubmed-article:7710065 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:7710065 | pubmed:day | 1 | lld:pubmed |
| pubmed-article:7710065 | pubmed:volume | 224 | lld:pubmed |
| pubmed-article:7710065 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:7710065 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:7710065 | pubmed:pagination | 166-72 | lld:pubmed |
| pubmed-article:7710065 | pubmed:dateRevised | 2006-11-15 | lld:pubmed |
| pubmed-article:7710065 | pubmed:meshHeading | pubmed-meshheading:7710065-... | lld:pubmed |
| pubmed-article:7710065 | pubmed:meshHeading | pubmed-meshheading:7710065-... | lld:pubmed |
| pubmed-article:7710065 | pubmed:meshHeading | pubmed-meshheading:7710065-... | lld:pubmed |
| pubmed-article:7710065 | pubmed:meshHeading | pubmed-meshheading:7710065-... | lld:pubmed |
| pubmed-article:7710065 | pubmed:meshHeading | pubmed-meshheading:7710065-... | lld:pubmed |
| pubmed-article:7710065 | pubmed:meshHeading | pubmed-meshheading:7710065-... | lld:pubmed |
| pubmed-article:7710065 | pubmed:year | 1995 | lld:pubmed |
| pubmed-article:7710065 | pubmed:articleTitle | Purification of glycosylphosphatidylinositol-anchored proteins by modified triton X-114 partitioning and preparative gel electrophoresis. | lld:pubmed |
| pubmed-article:7710065 | pubmed:affiliation | Department of Botany, University of Texas, Austin, 78713. | lld:pubmed |
| pubmed-article:7710065 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:7710065 | pubmed:publicationType | Research Support, U.S. Gov't, Non-P.H.S. | lld:pubmed |
| pubmed-article:7710065 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:7710065 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:7710065 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:7710065 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:7710065 | lld:pubmed |
