BIOMAT Database Logo BIOMAT Database Logo

Distributions of monooxygenase components and epoxide hydratase within the livers of untreated male rats. 1980

J A Redick, and T T Kawabata, and F P Guengerich, and P A Krieter, and T K Shires, and J Baron

UI MeSH Term Description Entries
D007118 Immunoassay A technique using antibodies for identifying or quantifying a substance. Usually the substance being studied serves as antigen both in antibody production and in measurement of antibody by the test substance. Immunochromatographic Assay,Assay, Immunochromatographic,Assays, Immunochromatographic,Immunoassays,Immunochromatographic Assays
D008099 Liver A large lobed glandular organ in the abdomen of vertebrates that is responsible for detoxification, metabolism, synthesis and storage of various substances. Livers
D008297 Male Males
D009251 NADPH-Ferrihemoprotein Reductase A flavoprotein that catalyzes the reduction of heme-thiolate-dependent monooxygenases and is part of the microsomal hydroxylating system. EC 1.6.2.4. Cytochrome P-450 Reductase,Ferrihemoprotein P-450 Reductase,NADPH Cytochrome P-450 Oxidoreductase,NADPH Cytochrome P-450 Reductase,NADPH Cytochrome c Reductase,Cytochrome P-450 Oxidase,Cytochrome P450 Reductase,Ferrihemoprotein P450 Reductase,NADPH Cytochrome P450 Oxidoreductase,NADPH Cytochrome P450 Reductase,NADPH-Cytochrome P450 Reductase,NADPH-P450 Reductase,Cytochrome P 450 Oxidase,Cytochrome P 450 Reductase,Ferrihemoprotein P 450 Reductase,NADPH Cytochrome P 450 Oxidoreductase,NADPH Cytochrome P 450 Reductase,NADPH Ferrihemoprotein Reductase,NADPH P450 Reductase,Oxidase, Cytochrome P-450,P-450 Oxidase, Cytochrome,P450 Reductase, Cytochrome,P450 Reductase, NADPH-Cytochrome,Reductase, Cytochrome P-450,Reductase, Cytochrome P450,Reductase, Ferrihemoprotein P-450,Reductase, Ferrihemoprotein P450,Reductase, NADPH-Cytochrome P450,Reductase, NADPH-Ferrihemoprotein,Reductase, NADPH-P450
D003577 Cytochrome P-450 Enzyme System A superfamily of hundreds of closely related HEMEPROTEINS found throughout the phylogenetic spectrum, from animals, plants, fungi, to bacteria. They include numerous complex monooxygenases (MIXED FUNCTION OXYGENASES). In animals, these P-450 enzymes serve two major functions: (1) biosynthesis of steroids, fatty acids, and bile acids; (2) metabolism of endogenous and a wide variety of exogenous substrates, such as toxins and drugs (BIOTRANSFORMATION). They are classified, according to their sequence similarities rather than functions, into CYP gene families (>40% homology) and subfamilies (>59% homology). For example, enzymes from the CYP1, CYP2, and CYP3 gene families are responsible for most drug metabolism. Cytochrome P-450,Cytochrome P-450 Enzyme,Cytochrome P-450-Dependent Monooxygenase,P-450 Enzyme,P450 Enzyme,CYP450 Family,CYP450 Superfamily,Cytochrome P-450 Enzymes,Cytochrome P-450 Families,Cytochrome P-450 Monooxygenase,Cytochrome P-450 Oxygenase,Cytochrome P-450 Superfamily,Cytochrome P450,Cytochrome P450 Superfamily,Cytochrome p450 Families,P-450 Enzymes,P450 Enzymes,Cytochrome P 450,Cytochrome P 450 Dependent Monooxygenase,Cytochrome P 450 Enzyme,Cytochrome P 450 Enzyme System,Cytochrome P 450 Enzymes,Cytochrome P 450 Families,Cytochrome P 450 Monooxygenase,Cytochrome P 450 Oxygenase,Cytochrome P 450 Superfamily,Enzyme, Cytochrome P-450,Enzyme, P-450,Enzyme, P450,Enzymes, Cytochrome P-450,Enzymes, P-450,Enzymes, P450,Monooxygenase, Cytochrome P-450,Monooxygenase, Cytochrome P-450-Dependent,P 450 Enzyme,P 450 Enzymes,P-450 Enzyme, Cytochrome,P-450 Enzymes, Cytochrome,Superfamily, CYP450,Superfamily, Cytochrome P-450,Superfamily, Cytochrome P450
D003580 Cytochromes Hemeproteins whose characteristic mode of action involves transfer of reducing equivalents which are associated with a reversible change in oxidation state of the prosthetic group. Formally, this redox change involves a single-electron, reversible equilibrium between the Fe(II) and Fe(III) states of the central iron atom (From Enzyme Nomenclature, 1992, p539). The various cytochrome subclasses are organized by the type of HEME and by the wavelength range of their reduced alpha-absorption bands. Cytochrome
D004851 Epoxide Hydrolases Enzymes that catalyze reversibly the formation of an epoxide or arene oxide from a glycol or aromatic diol, respectively. Epoxide Hydrase,Epoxide Hydrases,Epoxide Hydratase,Epoxide Hydratases,Epoxide Hydrolase,9,10-Epoxypalmitic Acid Hydrase,Microsomal Epoxide Hydrolase,Styrene Epoxide Hydrolase,9,10 Epoxypalmitic Acid Hydrase,Acid Hydrase, 9,10-Epoxypalmitic,Epoxide Hydrolase, Microsomal,Epoxide Hydrolase, Styrene,Hydrase, 9,10-Epoxypalmitic Acid,Hydrase, Epoxide,Hydrases, Epoxide,Hydratase, Epoxide,Hydratases, Epoxide,Hydrolase, Epoxide,Hydrolase, Microsomal Epoxide,Hydrolase, Styrene Epoxide,Hydrolases, Epoxide
D005288 Ferredoxins Iron-containing proteins that transfer electrons, usually at a low potential, to flavoproteins; the iron is not present as in heme. (McGraw-Hill Dictionary of Scientific and Technical Terms, 5th ed) Ferredoxin,Ferredoxin I,Ferredoxin II,Ferredoxin III
D006651 Histocytochemistry Study of intracellular distribution of chemicals, reaction sites, enzymes, etc., by means of staining reactions, radioactive isotope uptake, selective metal distribution in electron microscopy, or other methods. Cytochemistry
D000818 Animals Unicellular or multicellular, heterotrophic organisms, that have sensation and the power of voluntary movement. Under the older five kingdom paradigm, Animalia was one of the kingdoms. Under the modern three domain model, Animalia represents one of the many groups in the domain EUKARYOTA. Animal,Metazoa,Animalia

Related Publications

J A Redick, and T T Kawabata, and F P Guengerich, and P A Krieter, and T K Shires, and J Baron
An immunohistochemical study on the localization and distribution of epoxide hydrolase within livers of untreated rats.
November 1981, Molecular pharmacology,
J A Redick, and T T Kawabata, and F P Guengerich, and P A Krieter, and T K Shires, and J Baron
Monooxygenase and epoxide hydratase analysis by high-performance liquid chromatography.
June 1978, Analytical biochemistry,
J A Redick, and T T Kawabata, and F P Guengerich, and P A Krieter, and T K Shires, and J Baron
Differential control of rat microsomal "aryl hydrocarbon" monooxygenase and epoxide hydratase.
January 1976, The Journal of biological chemistry,
J A Redick, and T T Kawabata, and F P Guengerich, and P A Krieter, and T K Shires, and J Baron
Transplacental control of epoxide hydratase and its relationship to the control of microsomal monooxygenase.
May 1975, FEBS letters,
J A Redick, and T T Kawabata, and F P Guengerich, and P A Krieter, and T K Shires, and J Baron
The topology of epoxide hydratase and benzpyrene monooxygenase in the endoplasmic reticulum of rat liver.
September 1978, Biochimica et biophysica acta,
J A Redick, and T T Kawabata, and F P Guengerich, and P A Krieter, and T K Shires, and J Baron
An immunohistochemical study on the localization and distributions of phenobarbital- and 3-methylcholanthrene-inducible cytochromes P-450 within the livers of untreated rats.
June 1981, The Journal of biological chemistry,
J A Redick, and T T Kawabata, and F P Guengerich, and P A Krieter, and T K Shires, and J Baron
Kinetic behaviour of microsomal styrene monooxygenase and styrene epoxide hydratase in different animal species.
June 1977, Experientia,
J A Redick, and T T Kawabata, and F P Guengerich, and P A Krieter, and T K Shires, and J Baron
Improved syntheses of substrates for radiometric assays of microsomal monooxygenase (arylhydrocarbon hydroxylase) and epoxide hydratase.
April 1977, Analytical biochemistry,
J A Redick, and T T Kawabata, and F P Guengerich, and P A Krieter, and T K Shires, and J Baron
A specific gas chromatographic method for the determination of microsomal styrene monooxygenase and styrene epoxide hydratase activities.
April 1976, Journal of chromatography,
J A Redick, and T T Kawabata, and F P Guengerich, and P A Krieter, and T K Shires, and J Baron
Endogenous role of epoxide-hydratase. Development of a steroid epoxide-hydratase assay and properties of the enzyme.
June 1979, European journal of biochemistry,
Copied contents to your clipboard!