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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
8
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pubmed:dateCreated |
1981-6-23
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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).
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pubmed:grant | |
pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Aldehyde-Lyases,
http://linkedlifedata.com/resource/pubmed/chemical/Cytochrome P-450 Enzyme System,
http://linkedlifedata.com/resource/pubmed/chemical/Heme,
http://linkedlifedata.com/resource/pubmed/chemical/Hydroxyprogesterones,
http://linkedlifedata.com/resource/pubmed/chemical/Multienzyme Complexes,
http://linkedlifedata.com/resource/pubmed/chemical/Steroid 17-alpha-Hydroxylase,
http://linkedlifedata.com/resource/pubmed/chemical/Steroid Hydroxylases
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pubmed:status |
MEDLINE
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pubmed:month |
Apr
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pubmed:issn |
0021-9258
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
25
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pubmed:volume |
256
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
3871-6
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pubmed:dateRevised |
2007-11-14
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pubmed:meshHeading |
pubmed-meshheading:6971291-Aldehyde-Lyases,
pubmed-meshheading:6971291-Animals,
pubmed-meshheading:6971291-Animals, Newborn,
pubmed-meshheading:6971291-Cytochrome P-450 Enzyme System,
pubmed-meshheading:6971291-Heme,
pubmed-meshheading:6971291-Hydroxyprogesterones,
pubmed-meshheading:6971291-Kinetics,
pubmed-meshheading:6971291-Male,
pubmed-meshheading:6971291-Microsomes,
pubmed-meshheading:6971291-Multienzyme Complexes,
pubmed-meshheading:6971291-Spectrophotometry,
pubmed-meshheading:6971291-Steroid 17-alpha-Hydroxylase,
pubmed-meshheading:6971291-Steroid Hydroxylases,
pubmed-meshheading:6971291-Swine,
pubmed-meshheading:6971291-Testis
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pubmed:year |
1981
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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).
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.
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