Wild flowers -- England -- Oxfordshire -- Pictorial works. : A Victorian flower album : God's floral gems glistening on the verdant face of nature / collected and painted in the summer evenings of 1873 as a pleasing recreation by Henry Terry
Oxidants, Photochemical -- adverse effects. : International symposium on the biomedical effects of ozone and related photochemical oxidants / edited by S.D. Lee, M.G. Mustafa, M.A. Mehlman
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)
An enzyme that catalyzes the oxidative deamination of naturally occurring monoamines. It is a flavin-containing enzyme that is localized in mitochondrial membranes, whether in nerve terminals, the liver, or other organs. Monoamine oxidase is important in regulating the metabolic degradation of catecholamines and serotonin in neural or target tissues. Hepatic monoamine oxidase has a crucial defensive role in inactivating circulating monoamines or those, such as tyramine, that originate in the gut and are absorbed into the portal circulation. (From Goodman and Gilman's, The Pharmacological Basis of Therapeutics, 8th ed, p415) EC 1.4.3.4
An enzyme that catalyzes the oxidative deamination of naturally occurring monoamines. It is a flavin-containing enzyme that is localized in mitochondrial membranes, whether in nerve terminals, the liver, or other organs. Monoamine oxidase is important in regulating the metabolic degradation of catecholamines and serotonin in neural or target tissues. Hepatic monoamine oxidase has a crucial defensive role in inactivating circulating monoamines or those, such as tyramine, that originate in the gut and are absorbed into the portal circulation. (From Goodman and Gilman's, The Pharmacological Basis of Therapeutics, 8th ed, p415) EC 1.4.3.4
A large multisubunit protein complex found in the THYLAKOID MEMBRANE. It uses light energy derived from LIGHT-HARVESTING PROTEIN COMPLEXES to catalyze the splitting of WATER into DIOXYGEN and of reducing equivalents of HYDROGEN
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Oxidasen : Multi-copper oxidases / editor, Albrecht Messerschmidt
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
Amino acids -- Oxidation : Oxidation of amino acids, peptides, and proteins : kinetics and mechanism / Virender K. Sharma
2012
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Oxidation -- Australia. : P-Cymene and organic peroxides as indicators of oxidation in tea tree oil : a report for the Rural Industries Research and Development Corporation / by Ian Southwell
Oxidation -- Industrial applications : Liquid phase oxidation via heterogeneous catalysis : organic synthesis and industrial applications / edited by Mario G. Clerici, formerly with Enitecnologie (ENI Group) ; San Donato Milano, Italy, Oxana A. Kholdeeva, Boreskov Institute of Catalysis, Novosibirsk, Russia
Materials at high temperatures -- Oxidation -- Congresses : High-temperature oxidation and corrosion 2010 : selected, peer reviewed papers from the 3rd International Symposium on High-Temperature Oxidation and Corrosion 2010 (ISHOC-10), November 8-11, 2010, Zushi, Japan / edited by Toshio Maruyama [and others]
