| pubmed-article:3214436 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:3214436 | lifeskim:mentions | umls-concept:C1882726 | lld:lifeskim |
| pubmed-article:3214436 | lifeskim:mentions | umls-concept:C0034850 | lld:lifeskim |
| pubmed-article:3214436 | lifeskim:mentions | umls-concept:C0006774 | lld:lifeskim |
| pubmed-article:3214436 | lifeskim:mentions | umls-concept:C0332285 | lld:lifeskim |
| pubmed-article:3214436 | lifeskim:mentions | umls-concept:C1264633 | lld:lifeskim |
| pubmed-article:3214436 | pubmed:issue | 3 | lld:pubmed |
| pubmed-article:3214436 | pubmed:dateCreated | 1989-2-13 | lld:pubmed |
| pubmed-article:3214436 | pubmed:abstractText | The distribution of calmodulin-binding polypeptides in various rat liver subcellular fractions was investigated. Plasma-membrane, endosome, Golgi and lysosome fractions were prepared by established procedures. The calmodulin-binding polypeptides present in the subcellular fractions were identified by using an overlay technique after transfer from gels to nitrocellulose sheets. Distinctive populations of calmodulin-binding polypeptides were present in all the fractions examined except lysosomes. A major 115 kDa calmodulin-binding polypeptide of pI 4.3 was located to the endosome subfractions, and it emerges as a candidate endosome-specific protein. Partitioning of endosome fractions between aqueous and Triton X-114 phases indicated that the calmodulin-binding polypeptide was hydrophobic. Major calmodulin-binding polypeptides of 140 and 240 kDa and minor polypeptides of 40-60 kDa were present in plasma membranes. The distribution of calmodulin in the various endosome and plasma-membrane fractions was also analysed, and the results indicated that the amounts were high compared with those in the cytosol. | lld:pubmed |
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| pubmed-article:3214436 | pubmed:language | eng | lld:pubmed |
| pubmed-article:3214436 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:3214436 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:3214436 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:3214436 | pubmed:month | Nov | lld:pubmed |
| pubmed-article:3214436 | pubmed:issn | 0264-6021 | lld:pubmed |
| pubmed-article:3214436 | pubmed:author | pubmed-author:EvansW HWH | lld:pubmed |
| pubmed-article:3214436 | pubmed:author | pubmed-author:BachsOO | lld:pubmed |
| pubmed-article:3214436 | pubmed:author | pubmed-author:EnrickNN | lld:pubmed |
| pubmed-article:3214436 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:3214436 | pubmed:day | 1 | lld:pubmed |
| pubmed-article:3214436 | pubmed:volume | 255 | lld:pubmed |
| pubmed-article:3214436 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:3214436 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:3214436 | pubmed:pagination | 999-1005 | lld:pubmed |
| pubmed-article:3214436 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
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| pubmed-article:3214436 | pubmed:meshHeading | pubmed-meshheading:3214436-... | lld:pubmed |
| pubmed-article:3214436 | pubmed:year | 1988 | lld:pubmed |
| pubmed-article:3214436 | pubmed:articleTitle | A 115 kDa calmodulin-binding protein is located in rat liver endosome fractions. | lld:pubmed |
| pubmed-article:3214436 | pubmed:affiliation | Laboratory of Protein Structure, National Institute for Medical Research, London, U.K. | lld:pubmed |
| pubmed-article:3214436 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:3214436 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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