| pubmed-article:6971291 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:6971291 | lifeskim:mentions | umls-concept:C0021289 | lld:lifeskim |
| pubmed-article:6971291 | lifeskim:mentions | umls-concept:C0039005 | lld:lifeskim |
| pubmed-article:6971291 | lifeskim:mentions | umls-concept:C0039597 | lld:lifeskim |
| pubmed-article:6971291 | lifeskim:mentions | umls-concept:C1330957 | lld:lifeskim |
| pubmed-article:6971291 | lifeskim:mentions | umls-concept:C0010762 | lld:lifeskim |
| pubmed-article:6971291 | lifeskim:mentions | umls-concept:C0024188 | lld:lifeskim |
| pubmed-article:6971291 | lifeskim:mentions | umls-concept:C0033006 | lld:lifeskim |
| pubmed-article:6971291 | lifeskim:mentions | umls-concept:C1979928 | lld:lifeskim |
| pubmed-article:6971291 | lifeskim:mentions | umls-concept:C0596311 | lld:lifeskim |
| pubmed-article:6971291 | lifeskim:mentions | umls-concept:C1998793 | lld:lifeskim |
| pubmed-article:6971291 | lifeskim:mentions | umls-concept:C0871161 | lld:lifeskim |
| pubmed-article:6971291 | pubmed:issue | 8 | lld:pubmed |
| pubmed-article:6971291 | pubmed:dateCreated | 1981-6-23 | lld:pubmed |
| pubmed-article:6971291 | pubmed:abstractText | A cytochrome P-450 from neonatal pig testicular microsomes was purified to homogeneity as judged by electrophoresis on sodium dodecyl sulfate-polyacrylamide gels and by double diffusion on agar against antiserum raised in rabbits against the protein. The enzyme shows both 17 alpha-hydroxylase (Vmax = 4.6 nmol of product/min/nmol of P-450, Km = 1.5 microM) and C17,20 lyase (Vmax = 2.6 nmol of product/min/nmol of P-450, Km = 2.4 microM) activities. Both activities require NADPH and a flavoprotein P-450 reductase; microsomal P-450 reductase from pig and rat livers was used in these studies. The enzyme possesses a single subunit of molecular weight 59,000 +/- 1,000 as determined by electrophoresis on polyacrylamide with sodium dodecyl sulfate and by chromatography on sodium dodecyl sulfate-Sephadex. The enzyme is a glycoprotein and contains 8 nmol of heme/mg of protein and 40 nmol of phospholipid/mg of protein. All heme detected by pyridine hemochromogen is accounted for as P-450 by difference spectroscopy of the reduced P-450.carbon monoxide complex. This complex shows an absorbance maximum at 448 nm with no evidence of P-420. These studies raise the possibility that one microsomal protein (cytochrome P-450) may possess two enzymatic activities (hydroxylase and lyase). | lld:pubmed |
| pubmed-article:6971291 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:6971291 | pubmed:language | eng | lld:pubmed |
| pubmed-article:6971291 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:6971291 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:6971291 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:6971291 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:6971291 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:6971291 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:6971291 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:6971291 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:6971291 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:6971291 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:6971291 | pubmed:month | Apr | lld:pubmed |
| pubmed-article:6971291 | pubmed:issn | 0021-9258 | lld:pubmed |
| pubmed-article:6971291 | pubmed:author | pubmed-author:HaldP NPN | lld:pubmed |
| pubmed-article:6971291 | pubmed:author | pubmed-author:NakajinSS | lld:pubmed |
| pubmed-article:6971291 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:6971291 | pubmed:day | 25 | lld:pubmed |
| pubmed-article:6971291 | pubmed:volume | 256 | lld:pubmed |
| pubmed-article:6971291 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:6971291 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:6971291 | pubmed:pagination | 3871-6 | lld:pubmed |
| pubmed-article:6971291 | pubmed:dateRevised | 2007-11-14 | lld:pubmed |
| pubmed-article:6971291 | pubmed:meshHeading | pubmed-meshheading:6971291-... | lld:pubmed |
| pubmed-article:6971291 | pubmed:meshHeading | pubmed-meshheading:6971291-... | lld:pubmed |
| pubmed-article:6971291 | pubmed:meshHeading | pubmed-meshheading:6971291-... | lld:pubmed |
| pubmed-article:6971291 | pubmed:meshHeading | pubmed-meshheading:6971291-... | lld:pubmed |
| pubmed-article:6971291 | pubmed:meshHeading | pubmed-meshheading:6971291-... | lld:pubmed |
| pubmed-article:6971291 | pubmed:meshHeading | pubmed-meshheading:6971291-... | lld:pubmed |
| pubmed-article:6971291 | pubmed:meshHeading | pubmed-meshheading:6971291-... | lld:pubmed |
| pubmed-article:6971291 | pubmed:meshHeading | pubmed-meshheading:6971291-... | lld:pubmed |
| pubmed-article:6971291 | pubmed:meshHeading | pubmed-meshheading:6971291-... | lld:pubmed |
| pubmed-article:6971291 | pubmed:meshHeading | pubmed-meshheading:6971291-... | lld:pubmed |
| pubmed-article:6971291 | pubmed:meshHeading | pubmed-meshheading:6971291-... | lld:pubmed |
| pubmed-article:6971291 | pubmed:meshHeading | pubmed-meshheading:6971291-... | lld:pubmed |
| pubmed-article:6971291 | pubmed:meshHeading | pubmed-meshheading:6971291-... | lld:pubmed |
| pubmed-article:6971291 | pubmed:meshHeading | pubmed-meshheading:6971291-... | lld:pubmed |
| pubmed-article:6971291 | pubmed:meshHeading | pubmed-meshheading:6971291-... | lld:pubmed |
| pubmed-article:6971291 | pubmed:year | 1981 | lld:pubmed |
| pubmed-article:6971291 | pubmed:articleTitle | Microsomal cytochrome P-450 from neonatal pig testis. Purification and properties of A C21 steroid side-chain cleavage system (17 alpha-hydroxylase-C17,20 lyase). | lld:pubmed |
| pubmed-article:6971291 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:6971291 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:6971291 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:6971291 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:6971291 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:6971291 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:6971291 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:6971291 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:6971291 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:6971291 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:6971291 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:6971291 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:6971291 | lld:pubmed |
