By Trevor M. Penning, J. Mark Petrash

ISBN-10: 0841219702

ISBN-13: 9780841219700

ISBN-10: 0841238464

ISBN-13: 9780841238466

content material: part 1: basic review ; 1. creation and evaluate of the Aldo-Keto Reductase (AKR) Superfamily ; part 2: AKRS AND ENDOGENOUS TOXICANTS ; 2. Aldo-Keto Reductase-Catalyzed Detoxication of Endogenous Aldehydes linked to Diabetic problems ; three. Aldose Reductase Detoxifies Lipid Aldehydes and Their Glutathione Conjugates ; four. function of Aldose Reductase within the detoxing of Oxidized Phospholipids ; part three: AKRS AND EXOGENOUS TOXICANTS: TOBACCO comparable cancer causing agents ; five. Competing Roles of Reductases within the cleansing of the Tobacco-Specific Nitrosamine Ketone NNK ; 6. Aldo-Keto Reductases and the Metabolic Activation of Polycyclic fragrant Hydrocarbons ; 7. Molecular Cloning and Characterization of Dihydrodiol Dehydrogenase from Mouse ; eight effective Synthesis of the lively Metabolites of Carcinogenic Polycyclic fragrant Hydrocarbons ; nine. Chemistry of PAH o-Quinones Generated by means of the AKR Pathway of PAH Activation ; 10. research of Etheno-2'-Deoxyguanosine Adducts as Dosimeters of AKR Mediated Oxidative rigidity ; part four: AKRS AND EXOGENOUS TOXICANTS: MYCOTOXINS, ALDEHYDES AND KETONES ; eleven. Aflatoxin Aldehyde Reductases ; 12. Competing Reactions of Aflatoxin B1-Dialdehyde: Enzymatic relief vs Adduction with Lysine ; thirteen. using mammalian phone traces to enquire the function of aldo-keto reductases within the detoxication of aldehydes and ketones ; part five: AKRS, the tension reaction AND phone SIGNALING ; 14. Aldose Reductase and the strain reaction ; 15. Aldose Reductase Regulates Reactive Oxygen Species Mediated-Inflammatory indications ; sixteen. Aldo-Keto Reductases within the tension reaction of the Budding Yeast Saccharomyces cerevisiae

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Simply dialyzing AKR1B1 in the absence of cofactor will produce an oxidized form that can be converted back into the reduced form by treatment with DTT (24,24). The substrate properties of oxidized AKR1B1 differ markedly from those of reduced AKR1B1, as shown in Table III. Additional forms of AKR1B1 involving nitrosation or glutathionylation of C298 can be formed, each with unique kinetic properties (37,38). In general, any modification of AKR1B1 will decrease k^ /K values for any of the substrates.

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Aldo-Keto Reductases and Toxicant Metabolism by Trevor M. Penning, J. Mark Petrash


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