pubmed-article:6518166 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:6518166 | lifeskim:mentions | umls-concept:C1257890 | lld:lifeskim |
pubmed-article:6518166 | lifeskim:mentions | umls-concept:C0008377 | lld:lifeskim |
pubmed-article:6518166 | lifeskim:mentions | umls-concept:C0007452 | lld:lifeskim |
pubmed-article:6518166 | lifeskim:mentions | umls-concept:C0026237 | lld:lifeskim |
pubmed-article:6518166 | lifeskim:mentions | umls-concept:C1330957 | lld:lifeskim |
pubmed-article:6518166 | lifeskim:mentions | umls-concept:C0010762 | lld:lifeskim |
pubmed-article:6518166 | lifeskim:mentions | umls-concept:C1514562 | lld:lifeskim |
pubmed-article:6518166 | lifeskim:mentions | umls-concept:C1883221 | lld:lifeskim |
pubmed-article:6518166 | lifeskim:mentions | umls-concept:C1524075 | lld:lifeskim |
pubmed-article:6518166 | lifeskim:mentions | umls-concept:C1305923 | lld:lifeskim |
pubmed-article:6518166 | lifeskim:mentions | umls-concept:C0475264 | lld:lifeskim |
pubmed-article:6518166 | lifeskim:mentions | umls-concept:C0596311 | lld:lifeskim |
pubmed-article:6518166 | lifeskim:mentions | umls-concept:C0018966 | lld:lifeskim |
pubmed-article:6518166 | lifeskim:mentions | umls-concept:C0678594 | lld:lifeskim |
pubmed-article:6518166 | lifeskim:mentions | umls-concept:C1883204 | lld:lifeskim |
pubmed-article:6518166 | lifeskim:mentions | umls-concept:C1880389 | lld:lifeskim |
pubmed-article:6518166 | lifeskim:mentions | umls-concept:C0337112 | lld:lifeskim |
pubmed-article:6518166 | pubmed:issue | 3 | lld:pubmed |
pubmed-article:6518166 | pubmed:dateCreated | 1985-2-25 | lld:pubmed |
pubmed-article:6518166 | pubmed:abstractText | Cytochrome P-450scc consists of two domains linked with a short loop of the polypeptide chain; under hydrolysis by trypsin the domains retain their associated state due to rigid noncovalent interactions. A partial separation of the domains by gel-chromatography on Sephadex G-200 with retention of a haem group in domain I has been achieved after incubation of the trypsin-modified cytochrome P-450scc in 50 mM phosphate buffer (pH 7.2)/1 M NaCl/0.3% sodium cholate/0.3% Tween 80. The separation of domains I and II to individual fragments of the haemoprotein polypeptide chain has been achieved by chromatography under denaturation conditions on the activated thiopropyl-Sepharose via a selective covalent immobilization of domain II. Dissociation of a complex of domains I and II has been effectuated in the presence of 7 M guanidine. Structural characteristics of individual domains have been investigated. It is established that domain I containing a haem group is the N-terminal moiety, and domain II, the C-terminal moiety of the polypeptide chain of cytochrome P-450scc. The pathways of limited trypsinolysis of the native cytochrome P-450scc have been determined. The peptides containing cysteine residues localized on the surface of domain II and responsible for the interaction of haemoprotein with activated thiopropyl-Sepharose have been isolated in a homogeneous form and their amino-acid sequences have been assessed. | lld:pubmed |
pubmed-article:6518166 | pubmed:language | eng | lld:pubmed |
pubmed-article:6518166 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:6518166 | pubmed:citationSubset | IM | lld:pubmed |
pubmed-article:6518166 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:6518166 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:6518166 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:6518166 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:6518166 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:6518166 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:6518166 | pubmed:month | Dec | lld:pubmed |
pubmed-article:6518166 | pubmed:issn | 0006-3002 | lld:pubmed |
pubmed-article:6518166 | pubmed:author | pubmed-author:AkhremA AAA | lld:pubmed |
pubmed-article:6518166 | pubmed:author | pubmed-author:ShkumatovV... | lld:pubmed |
pubmed-article:6518166 | pubmed:author | pubmed-author:ChashchinV... | lld:pubmed |
pubmed-article:6518166 | pubmed:author | pubmed-author:LapkoV NVN | lld:pubmed |
pubmed-article:6518166 | pubmed:author | pubmed-author:AdamovichT... | lld:pubmed |
pubmed-article:6518166 | pubmed:author | pubmed-author:VasilevskyV... | lld:pubmed |
pubmed-article:6518166 | pubmed:author | pubmed-author:BerikbaevaT... | lld:pubmed |
pubmed-article:6518166 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:6518166 | pubmed:day | 21 | lld:pubmed |
pubmed-article:6518166 | pubmed:volume | 791 | lld:pubmed |
pubmed-article:6518166 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:6518166 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:6518166 | pubmed:pagination | 375-83 | lld:pubmed |
pubmed-article:6518166 | pubmed:dateRevised | 2004-11-17 | lld:pubmed |
pubmed-article:6518166 | pubmed:meshHeading | pubmed-meshheading:6518166-... | lld:pubmed |
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pubmed-article:6518166 | pubmed:meshHeading | pubmed-meshheading:6518166-... | lld:pubmed |
pubmed-article:6518166 | pubmed:year | 1984 | lld:pubmed |
pubmed-article:6518166 | pubmed:articleTitle | The domain structure of the cholesterol side-chain cleavage cytochrome P-450 from bovine adrenocortical mitochondria. Localization of haem group and domains in the polypeptide chain. | lld:pubmed |
pubmed-article:6518166 | pubmed:publicationType | Journal Article | lld:pubmed |
http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:6518166 | lld:pubmed |