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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
3
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pubmed:dateCreated |
1990-3-20
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pubmed:abstractText |
Six forms of cytochrome P-450 in the mitochondria of larvae from Musca domestica were isolated by solubilization with CHAPS followed by ammonium sulfate fractionation and HPLC on an anion-exchange column. Forms 1, 2, 3, 5, and 6 catalyzed the formation of 20-hydroxy-ecdysone from ecdysone in the presence of NADPH and pig adrenal adrenodoxin and adrenodoxin reductase at rates not much different that observed in mitochondria; whereas, fraction 4 showed an activity which was about 10-fold higher than mitochondria. Forms 4 and 5 were further purified by HPLC on a cation-exchange column followed by removal of excess detergent by hydroxyl apatite column chromatography. In vitro reconstitution of the monooxygenase activity confirmed that form 4 is primarily involved in the formation of 20-hydroxy-ecdysone from ecdysone. SDS-polyacrylamide gel electrophoresis indicated a high degree of purity of both forms 4 and 5, with molecular weights of 56 and 58 KDa, respectively.
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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/Aryl Hydrocarbon Hydroxylases,
http://linkedlifedata.com/resource/pubmed/chemical/Cytochrome P-450 Enzyme System,
http://linkedlifedata.com/resource/pubmed/chemical/Ecdysterone,
http://linkedlifedata.com/resource/pubmed/chemical/Steroid Hydroxylases,
http://linkedlifedata.com/resource/pubmed/chemical/ecdysone 20-hydroxylase
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pubmed:status |
MEDLINE
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pubmed:month |
Feb
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pubmed:issn |
0006-291X
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
14
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pubmed:volume |
166
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
1372-7
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pubmed:dateRevised |
2007-11-14
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pubmed:meshHeading |
pubmed-meshheading:2306250-Animals,
pubmed-meshheading:2306250-Aryl Hydrocarbon Hydroxylases,
pubmed-meshheading:2306250-Chromatography, High Pressure Liquid,
pubmed-meshheading:2306250-Cytochrome P-450 Enzyme System,
pubmed-meshheading:2306250-Ecdysterone,
pubmed-meshheading:2306250-Houseflies,
pubmed-meshheading:2306250-Larva,
pubmed-meshheading:2306250-Mitochondria,
pubmed-meshheading:2306250-Molecular Weight,
pubmed-meshheading:2306250-Steroid Hydroxylases
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pubmed:year |
1990
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pubmed:articleTitle |
Cytochrome P-450-catalyzed formation of 20-hydroxy-ecdysone in larval housefly mitochondria.
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pubmed:affiliation |
Department of Zoology, University of Georgia, Athens 30602.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.
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