Search results for "Cytochrome b5"

showing 8 items of 8 documents

Induction of rat hepatic epoxide hydratase by dietary antioxidants

1979

Abstract Supplementation of rat diet with butylated hydroxytoluene (BHT), butylated hydroxyanisole, or ethoxyquin resulted in increased liver epoxide hydratase activity. The increase was obvious at 0.1% and amounted to 200–400% at 0.5%. Increased activity was accompanied by increased proportion of the epoxide hydratase band in SDS polyacrylamide gels, indicating induction of the enzyme. Ethoxycoumarin deethylase activity and cytochrome b5 concentrations were moderately elevated while cytochrome P-450 concentrations and aryl hydrocarbon hydroxylase activity remained at control levels. Preferential inhibition of monooxygenase activity by metyrapone and not 7,8-benzoflavone, as well as increas…

MaleCytochromePopulationThymus GlandToxicologyAntioxidantsMixed Function Oxygenaseschemistry.chemical_compoundCytochrome b5AnimalsButylated hydroxytolueneDrug InteractionsBenzopyreneseducationEpoxide HydrolasesPharmacologychemistry.chemical_classificationeducation.field_of_studyEthoxyquinbiologyChemistryDNADietRatsEnzymeLiverBiochemistryEnzyme InductionMicrosomebiology.proteinButylated hydroxyanisoleToxicology and Applied Pharmacology
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Ethoxyquin as an inducer and inhibitor of phenobarbital-type cytochrome P-450 in rat liver microsomes.

1977

Abstract The effect of ethoxyquin in vivo and in vitro on drug metabolism in rat liver microsomes was studied. In feeding experiments, a threshold dose of induction was found at 0.05% ethoxyquin for 14 days. At 0.5% ethoxyquin, relative liver weight, cytochrome P-450 content, cytochrome b5 content, ethylmorphine demethylation, and ethoxycoumarin deethylation were increased by a factor of 1.5 to 2. Aryl hydrocarbon hydroxylase activity was, however, not induced but even decreased by 0.5% ethoxyquin in food. Induction of epoxide hydratase was marked, amounting to 400% of control after 0.5% ethoxyquin. The induced enzyme was similar to the phenobarbital-inducible cytochrome P-450 in its CO spe…

MaleCytochromeToxicologyMixed Function OxygenasesHydroxylationchemistry.chemical_compoundEthoxyquinCytochrome P-450 Enzyme SystemCytochrome b5AnimalsCytochrome P-450 Enzyme InhibitorsDemethylationPharmacologyEthoxyquinbiologyChemistryOrgan SizeMonooxygenaseRatsBiochemistryEnzyme InductionPhenobarbitalMicrosomebiology.proteinMicrosomes LiverQuinolinesElectrophoresis Polyacrylamide GelDrug metabolismToxicology and applied pharmacology
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Six amino acids define a minimal dimerization sequence and stabilize a transmembrane helix dimer by close packing and hydrogen bonding

2013

AbstractDistinct amino acid sequences have been described to mediate oligomerization of transmembrane α-helices. However, as the sequence context is crucial to determine specificity in transmembrane helix–helix interaction, the question arises how small a sequence can be without losing specificity. In the present analysis, six amino acids have been identified in the PsbF transmembrane helix dimer, which form the contact region of two interacting helices and are directly involved in helix–helix interactions. However, individual amino acids within the complex sequence pattern only together ensure sequence specificity of the analyzed transmembrane helix–helix interactions by mediating close pa…

Models MolecularStereochemistryDimerRecombinant Fusion ProteinsMolecular Sequence DataBiophysicsCytochrome b559Sequence (biology)Context (language use)Cytochrome b559BiologyBiochemistryProtein Structure Secondarychemistry.chemical_compoundBacterial ProteinsStructural BiologyGeneticsEscherichia coliProtein Interaction Domains and MotifsAmino Acid SequenceDimerization motifMolecular Biologychemistry.chemical_classificationSequence contextHydrogen bondProtein StabilityCell MembraneMembrane ProteinsHelix–helix interactionHydrogen BondingCell BiologyCytochrome b GroupTransmembrane proteinTransmembraneAmino acidTransmembrane domainchemistryDimerizationProtein BindingFEBS Letters
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Tonoplast subcellular localization of maize cytochrome b5 reductases

2000

Plant cytochrome b 5 reductases (b 5 R) are assumed to be part of an ER-associated redox chain that oxidizes NADH to provide electrons via cytochrome b5 (cyt b 5 ) to ER-associated fatty acyl desaturase and related hydroxylases, as in mammalian cells. Here we report on cDNA cloning of a novel maize b 5 R, NFR II, strongly related to a previously cloned cDNA, NFR I (Bagnaresi et al., 1999, Biochem, J. 338, 499-5051. Maize b 5 R isoforms are produced by a small multi-gene family. The NFR cDNAs were shown to encode active b 5 Rs by heterologous expression in yeast. Both reductases, in addition to Fe 3+ -chelates, efficiently reduced Cu 2+ -chelates. Using a polyclonal antibody able to recogniz…

DNA ComplementaryMolecular Sequence DataSaccharomyces cerevisiaePlant ScienceMolecular cloningBiologyPlant RootsZea maysIsozymeGene Expression Regulation EnzymologicComplementary DNACytochrome b5GeneticsAmino Acid SequenceMicroscopy ImmunoelectronCytochrome ReductasesCytochrome b5 reductaseSequence Homology Amino AcidCytochrome bSequence Analysis DNACell BiologySubcellular localizationMolecular biologyIsoenzymesBiochemistryVacuolesHeterologous expressionSequence AlignmentCytochrome-B(5) ReductaseThe Plant Journal
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Isoenzyme-specific phosphorylation of cytochromes P-450 and other drug metabolizing enzymes.

1987

Abstract A series of fourteen cytochrome P-450 isoenzymes was treated with three different protein kinases and found to devide into isoenzymes phosphorylated (i) by both the cyclic AMP-dependent kinase and the calcium-phospholipid-dependent kinase (P-450 PB 3a and PB 2e), (ii) by none of these kinases (P-450 PB 1b, MC 1b, UT 1, and thromboxane synthase), and (iii) by either the cyclic AMP-dependent kinase (P-450 LM 2, PB 2d, and PB 3b) or the calcium-phospholipid-dependent kinase (P-450 PB 1a, PB 2a, MC 1a, LM 3c, and LM 4). Other components of the monooxygenase system, cytochrome P-450 reductase, cytochrome b5, cytochrome b5 reductase as well as microsomal epoxide hydrolase, were poor subs…

CytochromeBiophysicsReductaseBiochemistrySubstrate SpecificityCytochrome P-450 Enzyme SystemCytochrome b5Cyclic AMPAnimalsPhosphorylationMolecular BiologyCytochrome b5 reductaseProtein Kinase CGlutathione TransferasebiologyChemistryKinaseCell BiologyMonooxygenaseMolecular biologyRatsIsoenzymesBiochemistryPharmaceutical PreparationsMicrosomal epoxide hydrolasebiology.proteinThromboxane-A synthaseRabbitsCasein KinasesProtein KinasesBiochemical and biophysical research communications
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Studies on the Biosynthesis of Microsomal Membrane Proteins. Site of Synthesis and Mode of Insertion of Cytochrome b5, Cytochrome b5 Reductase, Cytoc…

1982

The site of synthesis and mechanism of insertion into membranes of several microsomal polypeptides was studied using translation system programmed in vitro with polysomes or with mRNA extracted from free and membrane-bound rat liver polysomes. Primary translation products of cytochrome b5, NADH: cytochrome b5 oxidoreductase, NADPH: cytochrome P-450 oxidoreductase and epoxide hydrolase were isolated by specific immunoprecipitation and compared with the mature proteins. The following observations were made: 1 While cytochrome b5 and NADH: cytochrome b5 oxidoreductase are synthesized in free polysomes, NADPH: cytochrome P-450 oxidoreductase and epoxide hydrolase are made in membrane-bound poly…

MaleImmunodiffusionTime FactorsCytochromeBiochemistryElectron TransportCytochrome b5AnimalsCytochrome P450 family 1 member A1Epoxide hydrolaseCytochrome ReductasesCytochrome b5 reductaseNADPH-Ferrihemoprotein ReductaseEpoxide HydrolasesbiologyCytochrome bMembrane ProteinsCytochrome P450 reductaseRats Inbred StrainsMolecular biologyRatsCytochromes b5BiochemistryEnzyme InductionPhenobarbitalProtein BiosynthesisCoenzyme Q – cytochrome c reductaseMicrosomes Liverbiology.proteinCytochromesRabbitsCytochrome-B(5) ReductaseEuropean Journal of Biochemistry
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Effect of Antioxidants on Microsomal Enzymes of Rat Liver

1978

Rat diet was supplemented with butylated hydroxytoluene (BHT), butylated hydroxyanisole (BHA) or ethoxyquin (EQ) for 14 days, and hepatic microsomal epoxide hydratase (EH) and monooxygenase were subsequently studied in vitro. The antioxidants increased EH activity. The increase was marked with BHT (factor 3) and EQ (factor 4) and was paralleled by an increase in a protein band on SDS polyacrylamide gels which migrated together with purified rat hepatic EH. A slight but nonsignificant increase in cytochrome P450 content and a moderate increase in ethoxycoumarin deethylation and cytochrome b5 content was also observed while aryl hydrocarbon hydroxylase (AHH) activity was not elevated. Irrever…

education.field_of_studyEthoxyquinbiologyPopulationCytochrome P450Monooxygenasechemistry.chemical_compoundchemistryBiochemistryCytochrome b5biology.proteinMicrosomeButylated hydroxytolueneButylated hydroxyanisoleeducation
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Overexpression of CYB5R3 and NQO1, two NAD+-producing enzymes, mimics aspects of caloric restriction

2018

© 2018 The Authors.

0301 basic medicineAgingCalorie restrictionInflammationmedicine.disease_cause03 medical and health sciencesDownregulation and upregulationmedicineCytochrome b5 reductaseCalorie restrictionchemistry.chemical_classification030102 biochemistry & molecular biologybiologyCYB5R3Cell BiologyCell biology030104 developmental biologyEnzymechemistrySirtuinbiology.proteinNQO1NAD+ kinasemedicine.symptomCarcinogenesisMetabolic homeostasis
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