Switch to
| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
3
|
| pubmed:dateCreated |
1992-10-15
|
| pubmed:abstractText |
A cytochrome P-450 isozyme, P-450 bunitrolol (BTL), catalyzing bunitrolol 4-hydroxylation was partially purified from liver microsomes of adult male Sprague-Dawley rats by hydrophobic affinity chromatographic (omega-aminooctyl-Sepharose 4B) and high-performance liquid chromatographic (anion-exchange diethylaminoethyl-5PW) techniques. The specific content of the final preparation was 5.02 nmol/mg protein, which was 7.8-fold that of microsomes. It showed two protein bands of 49 and 32 kDa in sodium dodecylsulfate-polyacrylamide gel electrophoresis. N-Terminal 20 amino acid sequence of the protein of a higher molecular mass (49 kDa) isolated by an electroblotting technique is 94% homologous with that of CYP2D2. In a reconstituted system including NADPH-cytochrome P-450 reductase and an NADPH-generating system, the final preparation had the highest activity toward BTL and debrisoquine 4-hydroxylation among 12 isozymes of cytochrome P-450 examined. Kinetic parameters, KM and Vmax values, of P-450 BTL calculated for BTL 4-hydroxylation were 10.7 microM and 19.68 nmol/min/nmol P-450, respectively, whereas those values (mean +/- SE) of rat liver microsomes were 0.84 +/- 0.05 microM and 2.05 +/- 0.11 nmol/min/nmol P-450. When preincubated with rat liver microsomes, the antibody against the final P-450 BTL preparation suppressed bunitrolol and debrisoquine 4-hydroxylase activities dose-dependently and almost completely. These results suggest that cytochrome P-450 BTL and its immunochemically related P-450 isozyme(s) play a major role in debrisoquine 4-hydroxylation as well as in BTL 4-hydroxylation in rat liver microsomes.
|
| pubmed:language |
eng
|
| pubmed:journal | |
| pubmed:citationSubset |
IM
|
| pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Antibodies,
http://linkedlifedata.com/resource/pubmed/chemical/Cytochrome P-450 Enzyme System,
http://linkedlifedata.com/resource/pubmed/chemical/Isoenzymes,
http://linkedlifedata.com/resource/pubmed/chemical/Mixed Function Oxygenases,
http://linkedlifedata.com/resource/pubmed/chemical/Propanolamines,
http://linkedlifedata.com/resource/pubmed/chemical/bunitrolol 4-hydroxylase
|
| pubmed:status |
MEDLINE
|
| pubmed:issn |
0090-9556
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| pubmed:author | |
| pubmed:issnType |
Print
|
| pubmed:volume |
20
|
| pubmed:owner |
NLM
|
| pubmed:authorsComplete |
Y
|
| pubmed:pagination |
367-73
|
| pubmed:dateRevised |
2003-11-14
|
| pubmed:meshHeading |
pubmed-meshheading:1355709-Amino Acid Sequence,
pubmed-meshheading:1355709-Animals,
pubmed-meshheading:1355709-Antibodies,
pubmed-meshheading:1355709-Catalysis,
pubmed-meshheading:1355709-Chromatography, Affinity,
pubmed-meshheading:1355709-Chromatography, High Pressure Liquid,
pubmed-meshheading:1355709-Cytochrome P-450 Enzyme System,
pubmed-meshheading:1355709-Electrophoresis, Polyacrylamide Gel,
pubmed-meshheading:1355709-Hydroxylation,
pubmed-meshheading:1355709-Isoenzymes,
pubmed-meshheading:1355709-Kinetics,
pubmed-meshheading:1355709-Male,
pubmed-meshheading:1355709-Microsomes, Liver,
pubmed-meshheading:1355709-Mixed Function Oxygenases,
pubmed-meshheading:1355709-Molecular Sequence Data,
pubmed-meshheading:1355709-Propanolamines,
pubmed-meshheading:1355709-Rats,
pubmed-meshheading:1355709-Rats, Inbred Strains
|
| pubmed:articleTitle |
Purification and characterization of a cytochrome P-450 isozyme catalyzing bunitrolol 4-hydroxylation in liver microsomes of male rats.
|
| pubmed:affiliation |
Department of Biopharmaceutics, Faculty of Pharmaceutical Sciences, Chiba University, Japan.
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| pubmed:publicationType |
Journal Article
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