A fluorometric method to measure sublobular rates of mixed-function oxidation in the hemoglobin-free perfused rat liver. 1981

S Ji, and J J Lemasters, and R G Thurman

UI MeSH Term Description Entries
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
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
D010105 Oxygenases Oxidases that specifically introduce DIOXYGEN-derived oxygen atoms into a variety of organic molecules. Oxygenase
D010477 Perfusion Treatment process involving the injection of fluid into an organ or tissue. Perfusions
D003374 Coumarins Synthetic or naturally occurring substances related to coumarin, the delta-lactone of coumarinic acid. 1,2-Benzopyrone Derivatives,1,2-Benzopyrones,Coumarin Derivative,Coumarine,1,2-Benzo-Pyrones,Benzopyran-2-ones,Coumarin Derivatives,Coumarines,1,2 Benzo Pyrones,1,2 Benzopyrone Derivatives,1,2 Benzopyrones,Benzopyran 2 ones,Derivative, Coumarin,Derivatives, 1,2-Benzopyrone,Derivatives, Coumarin
D005260 Female Females
D005470 Fluorometry An analytical method for detecting and measuring FLUORESCENCE in compounds or targets such as cells, proteins, or nucleotides, or targets previously labeled with FLUORESCENCE AGENTS. Fluorimetry,Fluorometric Analysis,Analysis, Fluorometric
D006454 Hemoglobins The oxygen-carrying proteins of ERYTHROCYTES. They are found in all vertebrates and some invertebrates. The number of globin subunits in the hemoglobin quaternary structure differs between species. Structures range from monomeric to a variety of multimeric arrangements. Eryhem,Ferrous Hemoglobin,Hemoglobin,Hemoglobin, Ferrous
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
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

S Ji, and J J Lemasters, and R G Thurman
March 1981, The Journal of pharmacology and experimental therapeutics,
S Ji, and J J Lemasters, and R G Thurman
August 1971, Chemico-biological interactions,
S Ji, and J J Lemasters, and R G Thurman
January 1984, Biochemical pharmacology,
S Ji, and J J Lemasters, and R G Thurman
August 1973, Hoppe-Seyler's Zeitschrift fur physiologische Chemie,
S Ji, and J J Lemasters, and R G Thurman
September 1984, Hoppe-Seyler's Zeitschrift fur physiologische Chemie,
S Ji, and J J Lemasters, and R G Thurman
October 1969, European journal of biochemistry,
S Ji, and J J Lemasters, and R G Thurman
March 1970, Hoppe-Seyler's Zeitschrift fur physiologische Chemie,
S Ji, and J J Lemasters, and R G Thurman
October 1980, Archives of biochemistry and biophysics,
Copied contents to your clipboard!