0000000000179720

AUTHOR

Walter Wörner

showing 4 related works from this author

Time-dependence and differential induction of rat and guinea pig peroxisomal beta-oxidation, palmitoyl-CoA hydrolase, cytosolic and microsomal epoxid…

1988

Fischer-344 rats and Hartley guinea pigs received a diet containing 0.01% (w/w), 0.05% (w/w), or 0.25% (w/w) of the hypolipidemic drug fenofibrate. Rats were treated for 4, 7, 14, or 21 days, and a clear dose-dependent and weak time-dependent increase in liver/body weight ratio was observed. The specific activity of peroxisomal beta-oxidation increased linearly with time at all concentrations used. A dose-dependent increase in cEH was observed, but the activity remained constant after treatment for 7 days. Enhancement of palmitoyl-CoA hydrolase was dose-dependent, but was similar at all 4 time points investigated. In contrast to the other enzyme activities, mEH was not or only minimally (le…

MaleCancer Researchmedicine.medical_specialtyTime FactorsTiadenolGuinea PigsBiologyMicrobodiesGuinea pigCytosolInternal medicineMicrosomesHydrolasemedicineAnimalsHypolipidemic Agentschemistry.chemical_classificationEpoxide HydrolasesClofibrateFenofibrateGeneral MedicineRats Inbred F344RatsPalmitoyl-CoA hydrolaseEnzymeEndocrinologyOncologychemistryBiochemistryPalmitoyl-CoA HydrolaseMicrosomal epoxide hydrolaseEnzyme InductionThiolester Hydrolasesmedicine.drugJournal of cancer research and clinical oncology
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Rat Cytosolic Epoxide Hydrolase

1986

Rat liver microsomal and cytosolic epoxide hydrolase may be distinguished through differences in substrate specificity: styrene 7,8-oxide is preferentially hydrolyzed by the microsomal form, while trans-stilbene oxide is the prefered substrate for cytosolic epoxide hydrolase. Large interindividual differences in the specific activity of SpragueDawley (outbred strain) liver cytosolic epoxide hydrolase were observed, varying from 2 to 77 pmol/min x mg protein. Interindividual variations were much lower for microsomal epoxide hydrolase. The specific activity of Fischer F-344 (inbred strain) liver cytosolic epoxide hydrolase varied only by a factor of 2. The specific activity of cytosolic epoxi…

Epoxide hydrolase 2chemistry.chemical_compoundClofibratechemistryTiadenolBiochemistryMicrosomal epoxide hydrolaseStyrene oxidemedicineMicrosomeSpecific activityEpoxide hydrolasemedicine.drug
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Purification and characterization of rat-liver cytosolic epoxide hydrolase.

1988

Rat liver cytosolic epoxide hydrolase has been purified and characterized. The enzyme was purified from tiadenol-induced rat liver 540-fold with respect to trans-stilbene oxide as a substrate. Similar purification was obtained with the substrates trans-beta-ethyl styrene oxide and styrene 7,8-oxide, the specific activities decreasing in the order trans-beta-ethyl styrene oxide greater than styrene 7,8-oxide greater than trans-stilbene oxide. The enzyme exerts highest activity at pH 7.4 Km and Vmax of the pure enzyme for trans-stilbene oxide were 1.7 microM and 205 nmol x min-1 x mg protein-1 respectively. With trans-stilbene oxide as a substrate, the inhibition by organic solvents (2.5% by …

MaleGuinea PigsBiologyBiochemistryPeptide MappingStyreneSubstrate Specificitychemistry.chemical_compoundMiceCytosolStyrene oxideAnimalsIsoelectric PointEpoxide hydrolasechemistry.chemical_classificationEpoxide HydrolasesMolecular massHydrolysisImmunochemistrySubstrate (chemistry)Rats Inbred StrainsHydrogen-Ion ConcentrationRats Inbred F344RatsMice Inbred C57BLMolecular WeightEnzymechemistryBiochemistryLiverMicrosomal epoxide hydrolaseMicrosomeMicrosomes LiverSolventsPeptide HydrolasesEuropean journal of biochemistry
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Dihydrodiol dehydrogenase activities of rabbit liver are associated with hydroxysteroid dehydrogenases and aldo-keto reductases.

1992

1. Dihydrodiol dehydrogenase activities were investigated in rabbit liver. Using a five-step purification scheme, eight isoenzymes of dihydrodiol dehydrogenase with isoelectric points of 5.55-9.3 and promoter molecular masses of 34-35 kDa were purified to apparent homogeneity and designated CF-1 to CF-6, CM-1 and CM-2. 2. CF-1 and CF-2 had near-neutral isoelectric points of 7.4 and 6.8 and molecular masses of about 125 kDa in the native state. Both enzymes readily accepted NAD+ as well as NADP+ as coenzymes, had relatively low Km values of 0.33 mM and 0.47 mM for benzene dihydrodiol and resembled previously described carbonyl reductases in their substrate specificity towards ketones and qui…

MaleOxidoreductases Acting on CH-CH Group DonorsCarbonyl ReductaseStereochemistryAldo-Keto ReductasesDehydrogenaseReductaseBiochemistryCofactorCatalysisSubstrate SpecificityAldehyde Reductasepolycyclic compoundsAnimalsTissue DistributionIsoelectric PointAldehyde ReductaseAldo-keto reductasebiologyChemistryHydroxysteroid DehydrogenasesAntibodies MonoclonalHydroxysteroid DehydrogenasesIsoenzymesMolecular WeightAlcohol OxidoreductasesBiochemistryLiverbiology.proteinElectrophoresis Polyacrylamide GelNAD+ kinaseRabbitsOxidoreductasesEuropean journal of biochemistry
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