Switch to
Predicate | Object |
---|---|
rdf:type | |
lifeskim:mentions |
umls-concept:C0007452,
umls-concept:C0008377,
umls-concept:C0010762,
umls-concept:C0018966,
umls-concept:C0026237,
umls-concept:C0337112,
umls-concept:C0475264,
umls-concept:C0596311,
umls-concept:C0678594,
umls-concept:C1257890,
umls-concept:C1305923,
umls-concept:C1330957,
umls-concept:C1514562,
umls-concept:C1524075,
umls-concept:C1880389,
umls-concept:C1883204,
umls-concept:C1883221
|
pubmed:issue |
3
|
pubmed:dateCreated |
1985-2-25
|
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.
|
pubmed:language |
eng
|
pubmed:journal | |
pubmed:citationSubset |
IM
|
pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Cytochrome P-450 Enzyme System,
http://linkedlifedata.com/resource/pubmed/chemical/Heme,
http://linkedlifedata.com/resource/pubmed/chemical/Macromolecular Substances,
http://linkedlifedata.com/resource/pubmed/chemical/Peptide Fragments,
http://linkedlifedata.com/resource/pubmed/chemical/Trypsin
|
pubmed:status |
MEDLINE
|
pubmed:month |
Dec
|
pubmed:issn |
0006-3002
|
pubmed:author | |
pubmed:issnType |
Print
|
pubmed:day |
21
|
pubmed:volume |
791
|
pubmed:owner |
NLM
|
pubmed:authorsComplete |
Y
|
pubmed:pagination |
375-83
|
pubmed:dateRevised |
2004-11-17
|
pubmed:meshHeading |
pubmed-meshheading:6518166-Adrenal Cortex,
pubmed-meshheading:6518166-Amino Acid Sequence,
pubmed-meshheading:6518166-Animals,
pubmed-meshheading:6518166-Cattle,
pubmed-meshheading:6518166-Cytochrome P-450 Enzyme System,
pubmed-meshheading:6518166-Heme,
pubmed-meshheading:6518166-Macromolecular Substances,
pubmed-meshheading:6518166-Mitochondria,
pubmed-meshheading:6518166-Peptide Fragments,
pubmed-meshheading:6518166-Protein Binding,
pubmed-meshheading:6518166-Trypsin
|
pubmed:year |
1984
|
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.
|
pubmed:publicationType |
Journal Article
|