| pubmed-article:7332536 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:7332536 | lifeskim:mentions | umls-concept:C0042149 | lld:lifeskim |
| pubmed-article:7332536 | lifeskim:mentions | umls-concept:C0230445 | lld:lifeskim |
| pubmed-article:7332536 | lifeskim:mentions | umls-concept:C0008546 | lld:lifeskim |
| pubmed-article:7332536 | lifeskim:mentions | umls-concept:C1167622 | lld:lifeskim |
| pubmed-article:7332536 | lifeskim:mentions | umls-concept:C1704241 | lld:lifeskim |
| pubmed-article:7332536 | pubmed:issue | 1 | lld:pubmed |
| pubmed-article:7332536 | pubmed:dateCreated | 1982-4-20 | lld:pubmed |
| pubmed-article:7332536 | pubmed:abstractText | Various aspects of the interaction of oestrogen-receptor complexes with calf uterine chromatin covalently coupled to cellulose were analysed. Partially purified [3H]oestradiol-receptor complexes were bound to intact, or partially deproteinized, chromatin resins. Proteins were removed from the chromatin-cellulose resins by extraction with high molarities of salt, including NaCl/urea, guanidine hydrochloride and guanidine thiocyanate. After extensive washing to remove the salt, [3H]oestradiol-receptor-complex solutions were added to the resins and the degree of binding was determined. The extent of [3H]oestradiol-receptor-complex binding to chromatin was enhanced by extraction of chromosomal proteins. By varying the molarity of the salt, and consequently the extent of protein removal, it was possible to resolve [3H]oestradiol-receptor-complex binding to guanidine thiocyanate-extracted chromatin into two components. Similarly, [3H]oestradiol-receptor-complex binding to guanidine hydrochloride-treated chromatin included three regions of enhanced binding capacity. The [3H]oestradiol-receptor-chromatin interaction was saturable with respect to both intact and salt-extracted resins. Thus uterine chromatin may contain three or more specific classes of acceptors for the oestrogen-receptor complex. | lld:pubmed |
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| pubmed-article:7332536 | pubmed:language | eng | lld:pubmed |
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| pubmed-article:7332536 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:7332536 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:7332536 | pubmed:month | Oct | lld:pubmed |
| pubmed-article:7332536 | pubmed:issn | 0264-6021 | lld:pubmed |
| pubmed-article:7332536 | pubmed:author | pubmed-author:RuhT STS | lld:pubmed |
| pubmed-article:7332536 | pubmed:author | pubmed-author:RossPPJr | lld:pubmed |
| pubmed-article:7332536 | pubmed:author | pubmed-author:WoodD MDM | lld:pubmed |
| pubmed-article:7332536 | pubmed:author | pubmed-author:KeeneJ LJL | lld:pubmed |
| pubmed-article:7332536 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:7332536 | pubmed:day | 15 | lld:pubmed |
| pubmed-article:7332536 | pubmed:volume | 200 | lld:pubmed |
| pubmed-article:7332536 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:7332536 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:7332536 | pubmed:pagination | 133-42 | lld:pubmed |
| pubmed-article:7332536 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
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| pubmed-article:7332536 | pubmed:year | 1981 | lld:pubmed |
| pubmed-article:7332536 | pubmed:articleTitle | The binding of [3H]oestradiol-receptor complexes to calf uterine chromatin. | lld:pubmed |
| pubmed-article:7332536 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:7332536 | pubmed:publicationType | In Vitro | lld:pubmed |
| pubmed-article:7332536 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
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