Some effects of selenium deficiency on the hepatic microsomal cytochrome P-450 system in the rat. 1975

R F Burk, and B S Masters

UI MeSH Term Description Entries
D008297 Male Males
D008797 Metyrapone An inhibitor of the enzyme STEROID 11-BETA-MONOOXYGENASE. It is used as a test of the feedback hypothalamic-pituitary mechanism in the diagnosis of CUSHING SYNDROME. Methbipyranone,Methopyrapone,Metopiron,Metopirone,Métopirone,SU 4885
D008862 Microsomes, Liver Closed vesicles of fragmented endoplasmic reticulum created when liver cells or tissue are disrupted by homogenization. They may be smooth or rough. Liver Microsomes,Liver Microsome,Microsome, Liver
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
D010424 Pentobarbital A short-acting barbiturate that is effective as a sedative and hypnotic (but not as an anti-anxiety) agent and is usually given orally. It is prescribed more frequently for sleep induction than for sedation but, like similar agents, may lose its effectiveness by the second week of continued administration. (From AMA Drug Evaluations Annual, 1994, p236) Mebubarbital,Mebumal,Diabutal,Etaminal,Ethaminal,Nembutal,Pentobarbital Sodium,Pentobarbital, Monosodium Salt,Pentobarbitone,Sagatal,Monosodium Salt Pentobarbital
D010634 Phenobarbital A barbituric acid derivative that acts as a nonselective central nervous system depressant. It potentiates GAMMA-AMINOBUTYRIC ACID action on GABA-A RECEPTORS, and modulates chloride currents through receptor channels. It also inhibits glutamate induced depolarizations. Phenemal,Phenobarbitone,Phenylbarbital,Gardenal,Hysteps,Luminal,Phenobarbital Sodium,Phenobarbital, Monosodium Salt,Phenylethylbarbituric Acid,Acid, Phenylethylbarbituric,Monosodium Salt Phenobarbital,Sodium, Phenobarbital
D011485 Protein Binding The process in which substances, either endogenous or exogenous, bind to proteins, peptides, enzymes, protein precursors, or allied compounds. Specific protein-binding measures are often used as assays in diagnostic assessments. Plasma Protein Binding Capacity,Binding, Protein
D003486 Cyanides Inorganic salts of HYDROGEN CYANIDE containing the -CN radical. The concept also includes isocyanides. It is distinguished from NITRILES, which denotes organic compounds containing the -CN radical. Cyanide,Isocyanide,Isocyanides
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

Related Publications

R F Burk, and B S Masters
June 1987, Journal of applied toxicology : JAT,
R F Burk, and B S Masters
December 1990, Journal of UOEH,
R F Burk, and B S Masters
January 1986, Journal of pharmacobio-dynamics,
R F Burk, and B S Masters
October 1980, Biochemical pharmacology,
R F Burk, and B S Masters
May 1977, Tanpakushitsu kakusan koso. Protein, nucleic acid, enzyme,
R F Burk, and B S Masters
November 1968, Hoppe-Seyler's Zeitschrift fur physiologische Chemie,
R F Burk, and B S Masters
July 1970, Biochemical pharmacology,
R F Burk, and B S Masters
February 1983, The Journal of biological chemistry,
R F Burk, and B S Masters
January 1984, Annals of the New York Academy of Sciences,
Copied contents to your clipboard!