Search results for "Ketosteroid"

showing 4 items of 4 documents

Genetically engineered V79 chinese hamster cell expression of purified cytochromeP-450iib1 monooxygenase activity

1989

Chinese hamster V79 fibroblasts, frequently used as target cells in short-term tests for mutagenicity, do not possess measurable monooxygenase activity; in particular, enzymatic oxidation of testosterone (T) cannot be demonstrated. If these V79 cells, however, had been transfected with the cDNA-encoding rat liver cytochrome P-450IIB1 under control of the SV40 early promoter, they stably expressed monooxygenase activity. These so-called SD1 cells then oxidatively metabolized T at a rate of 27 pmol/mg protein/min, converting it to 16 alpha- and 16 beta-hydroxy-T as well as 4-androsten-3,17-dione as sole metabolites in a ratio of 1.1:1.0:1.6. The regio- and stereoselective conversion of T by S…

MaleOxygenaseCytochromeCellTransfectionToxicologyIsozymeChinese hamsterCricetulusCytochrome P-450 Enzyme SystemCricetinaemedicineAnimalsTestosteroneCells CulturedChromatography High Pressure Liquidchemistry.chemical_classificationbiologyRats Inbred StrainsTransfectionKetosteroidsbiology.organism_classificationMolecular biologyRatsIsoenzymesmedicine.anatomical_structureEnzymeBiochemistrychemistryPhenobarbitalMicrosomes LiverOxygenasesbiology.proteinCricetulusGenetic EngineeringOxidation-ReductionJournal of Biochemical Toxicology
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Structure of Rhodococcus erythropolis limonene-1,2-epoxide hydrolase reveals a novel active site

2003

Epoxide hydrolases are essential for the processing of epoxide-containing compounds in detoxification or metabolism. The classic epoxide hydrolases have an alpha/beta hydrolase fold and act via a two-step reaction mechanism including an enzyme-substrate intermediate. We report here the structure of the limonene-1,2-epoxide hydrolase from Rhodococcus erythropolis, solved using single-wavelength anomalous dispersion from a selenomethionine-substituted protein and refined at 1.2 A resolution. This enzyme represents a completely different structure and a novel one-step mechanism. The fold features a highly curved six-stranded mixed beta-sheet, with four alpha-helices packed onto it to create a …

Models MolecularAFSG Stafafdelingen (WUATV)10050 Institute of Pharmacology and Toxicologydrug protein bindingEnantioselectivityEpoxide hydrolaseCrystallography X-Rayuncultured actinomyceteCatalytic Domain2400 General Immunology and Microbiologyalpha helixRhodococcuscholesterol epoxide hydrolasenaphthalene 12-dioxygenasedcl14limonene 12 epoxide hydrolaseEpoxide hydrolaseBacteria (microorganisms)delta(5)-3-ketosteroid isomeraseEpoxide HydrolasesLimonene-12-epoxide hydrolaseGeneral Neurosciencearticle2800 General NeuroscienceActinobacteria (class)Articlesagrobacterium-radiobacterEnzyme structureRecombinant Proteinsunclassified drugenzyme structurereaction analysisBiochemistrypriority journalenzyme active siteMechanism2-dioxygenaseDimerizationBiotechnologychemical reactioncrystal structureaspergillus-nigermacromolecular structuresStereochemistrybeta sheetvalpromideMolecular Sequence Data610 Medicine & healthGenetics and Molecular BiologyBiologyGeneral Biochemistry Genetics and Molecular BiologyBacterial Proteinssite directed mutagenesis1300 General Biochemistry Genetics and Molecular BiologyHydrolase1312 Molecular BiologyAmino Acid SequencedetoxificationRhodococcus erythropolisBiologyMonoterpene degradationMolecular Biologyprotein data-bankenzyme substrate complexEnzyme substrate complexnonhumancatalysisSequence Homology Amino AcidGeneral Immunology and Microbiologybacterial enzymeActive sitecrystal-structureAFSG Staff Departments (WUATV)enzyme metabolismProtein SubunitsenzymeEpoxide HydrolasesGeneral Biochemistrybiology.proteinMutagenesis Site-Directed570 Life sciences; biologyselenomethioninenaphthalene 1Alpha helix
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Determination of ketosteroid hormones in meat by liquid chromatography tandem mass spectrometry and derivatization chemistry.

2015

A method for the determination and quantification of ketosteroid hormones in meat by mass spectrometry, based on the derivatization of the carbonyl moiety of steroids by O-methylhydroxylamine, is presented. The quantitative assay is performed by means of multiple-reaction-monitoring (MRM) scan mode and using the corresponding labelled species, obtained by reaction with d 3-methoxylamine, as internal standard. The accuracy of the method was established by evaluating artificially spiked samples, obtaining values in the range 90-110%. Recovery tests were performed on blank matrix samples spiked with non-natural steroids including trenbolone and melengestrol acetate. The latter experiment revea…

Multiple reaction monitoringChromatographyMeatMass spectrometrySelected reaction monitoringKetosteroidMass spectrometrySolid-phase microextractionKetosteroidsBiochemistryAnalytical ChemistryMatrix (chemical analysis)chemistry.chemical_compoundTrenbolonechemistryLiquid chromatography–mass spectrometryTandem Mass SpectrometryKetosteroidMethoxylamineUHPLCmedicineDerivatizationSolid Phase Microextractionmedicine.drugAnalytical and bioanalytical chemistry
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Die C-17-Ketosteroidausschüttung nach Gaben von Äthanol und Wein

1955

Single or repeated doses of wine result in a statistically significant rise of excretion of C-17-Cetosteroids. After application of the same quantity of ethylalcohol, this effect was not seen. These results can be correlated with former observations on the changes of the nuclei-volumes of the zona fasciculata.

PharmacologyWineendocrine systemmedicine.medical_specialtyEthanolfood and beveragesCell BiologyUrineExcretionCellular and Molecular Neurosciencechemistry.chemical_compoundEndocrinologymedicine.anatomical_structurechemistryZona fasciculataRepeated dosesInternal medicineKetosteroidmedicineMolecular MedicineMolecular BiologyExperientia
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