pubmed-article:6745440 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:6745440 | lifeskim:mentions | umls-concept:C0086418 | lld:lifeskim |
pubmed-article:6745440 | lifeskim:mentions | umls-concept:C0024264 | lld:lifeskim |
pubmed-article:6745440 | lifeskim:mentions | umls-concept:C1383501 | lld:lifeskim |
pubmed-article:6745440 | lifeskim:mentions | umls-concept:C0086045 | lld:lifeskim |
pubmed-article:6745440 | lifeskim:mentions | umls-concept:C0037494 | lld:lifeskim |
pubmed-article:6745440 | lifeskim:mentions | umls-concept:C1280500 | lld:lifeskim |
pubmed-article:6745440 | lifeskim:mentions | umls-concept:C0242210 | lld:lifeskim |
pubmed-article:6745440 | lifeskim:mentions | umls-concept:C0871161 | lld:lifeskim |
pubmed-article:6745440 | lifeskim:mentions | umls-concept:C0066695 | lld:lifeskim |
pubmed-article:6745440 | pubmed:issue | 2 | lld:pubmed |
pubmed-article:6745440 | pubmed:dateCreated | 1984-9-20 | lld:pubmed |
pubmed-article:6745440 | pubmed:abstractText | Side chain-hydroxylated derivatives of cholesterol (OH sterol) inhibiting lymphoblastic transformation bind with high affinity and specificity to a hydroxysterol binding protein (OHSBP) in the cytosol of human lymphocytes. These binding properties of OHSBP suggested some analogies with that of steroid hormone receptors. The observation of a nuclear binding of 25-OH[3H]cholesterol prompted us to apply to the cytosolic OH sterol-OHSBP complex the physico-chemical treatments known to 'activate' the steroid hormone receptors. A change of sedimentation coefficient from 8.3 to 4.3 S was observed in hypertonic buffer (0.4 M KCl) but the resulting 4.3 S complex dissociates easily whereas the 'native' 8.3 S form does not. Moreover, molybdate did not prevent the 8.3----4.3 S transformation induced by KCl and neither ammonium sulfate precipitation nor increasing temperature had any effect on the sedimentation coefficient of the 8.3 S complex. Thus, several physico-chemical features differentiate the OH sterol-OHSBP complex from steroid hormone receptors. | lld:pubmed |
pubmed-article:6745440 | pubmed:language | eng | lld:pubmed |
pubmed-article:6745440 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:6745440 | pubmed:citationSubset | IM | lld:pubmed |
pubmed-article:6745440 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:6745440 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:6745440 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:6745440 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:6745440 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:6745440 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:6745440 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:6745440 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:6745440 | pubmed:month | Aug | lld:pubmed |
pubmed-article:6745440 | pubmed:issn | 0014-5793 | lld:pubmed |
pubmed-article:6745440 | pubmed:author | pubmed-author:Crastes de... | lld:pubmed |
pubmed-article:6745440 | pubmed:author | pubmed-author:DescompsBB | lld:pubmed |
pubmed-article:6745440 | pubmed:author | pubmed-author:AstrucMM | lld:pubmed |
pubmed-article:6745440 | pubmed:author | pubmed-author:DefayRR | lld:pubmed |
pubmed-article:6745440 | pubmed:author | pubmed-author:BesemeFF | lld:pubmed |
pubmed-article:6745440 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:6745440 | pubmed:day | 6 | lld:pubmed |
pubmed-article:6745440 | pubmed:volume | 173 | lld:pubmed |
pubmed-article:6745440 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:6745440 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:6745440 | pubmed:pagination | 319-26 | lld:pubmed |
pubmed-article:6745440 | pubmed:dateRevised | 2006-11-15 | lld:pubmed |
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pubmed-article:6745440 | pubmed:year | 1984 | lld:pubmed |
pubmed-article:6745440 | pubmed:articleTitle | Physico-chemical properties of the hydroxysterol binding protein of human lymphocyte cytosol. Effects of high salt concentrations and molybdate. | lld:pubmed |
pubmed-article:6745440 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:6745440 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |