Sequential administrations of polyriboinosinic acid and polyribocytidylic acid induce interferon and depress the hepatic cytochrome P-450-dependent monooxygenase system. 1982

L B Deloria, and G J Mannering

UI MeSH Term Description Entries
D007369 Interferon Inducers Agents that promote the production and release of interferons. They include mitogens, lipopolysaccharides, and the synthetic polymers Poly A-U and Poly I-C. Viruses, bacteria, and protozoa have been also known to induce interferons. Inducers, Interferon
D007372 Interferons Proteins secreted by vertebrate cells in response to a wide variety of inducers. They confer resistance against many different viruses, inhibit proliferation of normal and malignant cells, impede multiplication of intracellular parasites, enhance macrophage and granulocyte phagocytosis, augment natural killer cell activity, and show several other immunomodulatory functions. Interferon
D008297 Male Males
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
D010088 Oxidoreductases The class of all enzymes catalyzing oxidoreduction reactions. The substrate that is oxidized is regarded as a hydrogen donor. The systematic name is based on donor:acceptor oxidoreductase. The recommended name will be dehydrogenase, wherever this is possible; as an alternative, reductase can be used. Oxidase is only used in cases where O2 is the acceptor. (Enzyme Nomenclature, 1992, p9) Dehydrogenases,Oxidases,Oxidoreductase,Reductases,Dehydrogenase,Oxidase,Reductase
D011066 Poly C A group of cytosine ribonucleotides in which the phosphate residues of each cytosine ribonucleotide act as bridges in forming diester linkages between the ribose moieties. Cytosine Polynucleotides,Polycytidylic Acid,Polycytidylic Acids,Acid, Polycytidylic,Acids, Polycytidylic,Polynucleotides, Cytosine
D011069 Poly I A group of inosine ribonucleotides in which the phosphate residues of each inosine ribonucleotide act as bridges in forming diester linkages between the ribose moieties. Inosine Polynucleotides,Polyinosinic Acids,Acids, Polyinosinic,Polynucleotides, Inosine
D011131 Polyribonucleotides A group of 13 or more ribonucleotides in which the phosphate residues of each ribonucleotide act as bridges in forming diester linkages between the ribose moieties.
D005037 Ethylmorphine-N-Demethylase A drug-metabolizing enzyme of the hepatic microsomal oxidase system which catalyzes the oxidation of the N-methyl group of ethylmorphine with the formation of formaldehyde. Ethylmorphine N Demethylase,Demethylase, Ethylmorphine N,N Demethylase, Ethylmorphine
D006899 Mixed Function Oxygenases Widely distributed enzymes that carry out oxidation-reduction reactions in which one atom of the oxygen molecule is incorporated into the organic substrate; the other oxygen atom is reduced and combined with hydrogen ions to form water. They are also known as monooxygenases or hydroxylases. These reactions require two substrates as reductants for each of the two oxygen atoms. There are different classes of monooxygenases depending on the type of hydrogen-providing cosubstrate (COENZYMES) required in the mixed-function oxidation. Hydroxylase,Hydroxylases,Mixed Function Oxidase,Mixed Function Oxygenase,Monooxygenase,Monooxygenases,Mixed Function Oxidases,Function Oxidase, Mixed,Function Oxygenase, Mixed,Oxidase, Mixed Function,Oxidases, Mixed Function,Oxygenase, Mixed Function,Oxygenases, Mixed Function

Related Publications

L B Deloria, and G J Mannering
November 1976, Biochemical and biophysical research communications,
L B Deloria, and G J Mannering
February 1989, Japanese journal of pharmacology,
L B Deloria, and G J Mannering
January 1982, Comparative biochemistry and physiology. B, Comparative biochemistry,
L B Deloria, and G J Mannering
January 1986, Zeitschrift fur Naturforschung. C, Journal of biosciences,
L B Deloria, and G J Mannering
May 1979, Toxicology and applied pharmacology,
Copied contents to your clipboard!