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Molecular Aspects of Oxidative Drug Metabolizing Enzymes: by Emel Arinc, John B. Schenkman, Ernest Hodgson

By Emel Arinc, John B. Schenkman, Ernest Hodgson

Presented listed below are contemporary advances in biochemical, toxicological, and regulatory points of oxidative drug metabolizing enzymes. ordinarily cytochrome P450-dependent and flavin-containing monooxygenases (FMO) are lined. additionally, the e-book bargains with genotoxicity reports and toxicological interactions of environmental chemical compounds and mechanisms of mutagenicity and tumor formation. the development of genetically engineered mammalian cells for the construction of a particular P450 isozyme and the appliance of those phone traces in drug metabolism, mutagenicity and toxicity reviews are defined intimately. additional, perception is supplied into how a couple of aquatic species focus on pollution and their genotoxicity.

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Additional info for Molecular Aspects of Oxidative Drug Metabolizing Enzymes: Their Significance in Environmental Toxicology, Chemical Carcinogenesis and Health

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5). On the other hand, the evidence obtained by Phillips and Langdon (1962) and Baggott and Langdon (1970) suggested that a random mechanism operates for the reaction catalyzed 29 40 -.. o Q. >01 .... e - .... & IJ[NADPHI (pM-I) Fig. 3. Double reciprocal plots of the initial velocity for the reduction of cytochrome c by the purified sheep liver reductase as a function of NADPH at different concentrations of cytochrome c. 4 11M (~-~), 127 11M (0-0) and 171 11M (e-e). 027 units of the purified sheep liver reductase.

The points are the means of two different sets of data and each point is the mean of duplicate determinations. The lines are derived using linear regression. ;: (1988), with permission. by the purified pig liver reductase. Subsequent to these proposals, a sequential ordered mechanism reported by Dignam and Strobel (1977) and Kobayashi and Rikans (1984) for the interaction of co-substrates with the rat and guinea pig liver microsomal cytochrome P450 reductases, respectively. In a view of the apparently contradictory data in the literature surrounding cytochrome P450 reductase kinetic mechanism with NADPH and cytochrome c, the ping-pong kinetic mechanism proposed for sheep liver and lung cytochrome P450 reductases (i~can and Annr;, 1986, 1988) is in good agreement with the conclusions obtained for purified pig liver microsomal 30 30 2S N b "i .

1992). 24 The presence of variable amounts of proteolytically cleaved smaller molecular weight inactive reductases has been reported in the purified rabbit liver (French and Coon, 1979), rabbit lung (Serabjit-Singh et al. 1979), pig liver (Yasukochi et al. 1980), guinea pig liver (Kobayashi and Rikans, 1984) and sheep liver and lung (i~can and Annt;:, 1986, 1988) amphipathic reductase preparations. Recently, an unusual proteolytic cleavage at the Asn-Gly (residues 502-503) linkage of the 676 residue of pig liver reductase has been reported (Haniu et al.

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