Hepatic Microsomal Ethanol-oxidizing System
نویسندگان
چکیده
منابع مشابه
Hepatic Microsomal Alcohol-oxidizing System
Oxidation of methanol, ethanol, propanol, and butanol by the microsomal fraction of rat liver homogenate is described. This microsomal alcohol-oxidizing system is dependent on NADPH and molecular oxygen and is partially inhibited by CO, features which are commori for microsomal drug-metabolizing enzymes. The activity of the microsomal alcohol-oxidizing system could be dissociated from the alcoh...
متن کاملReconstitution of the Microsomal Ethanol-oxidizing System
An ethanol-oxidizing system was reconstituted with cytochrome P-450, NADPH-cytochrome r reductase, and phospholipid. This system also metabolized propanol, butanol, and benzphetamine. Neither catalase nor alcohol dehydrogenase plays a role in this system. Characteristics of this system are similar to those of the microsomal ethanoloxidizing system. Chronic ethanol feeding of either male or fema...
متن کاملHepatic Microsomal Ethanol-oxidizing System IN WTRO CHARACTERISTICS AND ADAPTIVE PROPERTIES IN VIVO*
A hepatic microsomal ethanol-oxidizing system is described both in men and rats. It is distinguished from alcohol dehydrogenase by its subcellular localization (cytosol for alcohol dehydrogenase, microsomes for this system), its pH optimum (physiological pH versus pH 10 to 11 for alcohol dehydrogenase), and its cofactor requirements (NADPH versus NAD+ for alcohol dehydrogenase). It also require...
متن کاملHepatic microsomal ethanol-oxidizing system. In vitro characteristics and adaptive properties in vivo.
A hepatic microsomal ethanol-oxidizing system is described both in men and rats. It is distinguished from alcohol dehydrogenase by its subcellular localization (cytosol for alcohol dehydrogenase, microsomes for this system), its pH optimum (physiological pH versus pH 10 to 11 for alcohol dehydrogenase), and its cofactor requirements (NADPH versus NAD+ for alcohol dehydrogenase). It also require...
متن کاملThe microsomal ethanol oxidizing system: its role in ethanol and xenobiotic metabolism.
After chronic ethanol consumption, the activity of the microsomal ethanol-oxidizing system (MEOS) increases and contributes to ethanol tolerance, as most conclusively shown in alcohol-dehydrogenase-negative deermice. In man and animals, there is an associated rise in microsomal cytochrome P-450, including a specific form (P-450IIEI) with high affinity for ethanol and for the activation of some ...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 1970
ISSN: 0021-9258
DOI: 10.1016/s0021-9258(18)63099-6