1966
DOI: 10.1097/00006842-196607000-00018
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Alcohol Dehydrogenase in Ethanol Metabolism

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Cited by 27 publications
(3 citation statements)
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“…Aus Rhesusaffenleber sind zwei Isoenzyme der ADH isoliert worden, welche sich in Bezug auf verschiedene physikalisch-chemische und katalytische Parameter unterscheiden [12,27]. Multiple molekulare Formen der ADH sind ferner bei Drosophila melanogaster [6,18], von Pflanzen [14,17] nachgewiesen Hefe [10,15] …”
Section: Heterogeneity and Tissue Distribution Of Alcohol Dehydrogenaunclassified
“…Aus Rhesusaffenleber sind zwei Isoenzyme der ADH isoliert worden, welche sich in Bezug auf verschiedene physikalisch-chemische und katalytische Parameter unterscheiden [12,27]. Multiple molekulare Formen der ADH sind ferner bei Drosophila melanogaster [6,18], von Pflanzen [14,17] nachgewiesen Hefe [10,15] …”
Section: Heterogeneity and Tissue Distribution Of Alcohol Dehydrogenaunclassified
“…Although low concentration of alcohol stimulates the activity of hepatic ADH, high concentration of alcohol inhibits it [15]. In this study, a high dose (0.15 mL/100 mg) of Hongxing liquor (containing 65% ethanol) Pretreatment with ECR suppressed the inhibitory effect of high alcohol content on hepatic ADH activity (Fig 2A).…”
Section: Effect Of Ecr On Hepatic Adh and Aldh Activitiesmentioning
confidence: 49%
“…An interpretation of this result has to be tentative, but it may be sought in the fact that wild rats, in contrast to domestic rats, have large adrenal 320 glands. The adrenal glands generate adrenal-cortical steroids, one of which is alcohol dehydrogenase (ADH), which oxidizes alcohol in the liver (von Wartburg & Papenberg, 1966). It is conceivable that during the exposure phase of the experiment, alcohol ingestion in the wild rats was limited only by their liquid requirement, and that these animals, due to the size of their adrenal glands, are capable of metabolizing ethanol at a higher rate than domestic rats could.…”
Section: Discussionmentioning
confidence: 99%