Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
6
pubmed:dateCreated
1991-5-20
pubmed:abstractText
Two types of alcohol dehydrogenase isoenzymes (differing in their affinity for ethanol, sensitivity to 4-methylpyrazole, and electrophoretic migration) have been identified in the human stomach. At the high ethanol concentrations prevailing in the gastric lumen during alcohol consumption, the sum of their activities could account for significant oxidation of ethanol. In vitro, these activities were inhibited by cimetidine and ranitidine, but not by famotidine. In vivo, therapeutic doses of cimetidine (but not of famotidine) increased blood ethanol levels when ethanol was given orally, but not when it was given intravenously, indicating a significant contribution of the gastric ADH to the bioavailability and thereby the potential toxicity of ethanol.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Dec
pubmed:issn
0145-6008
pubmed:author
pubmed:issnType
Print
pubmed:volume
14
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
946-50
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed:year
1990
pubmed:articleTitle
Human gastric alcohol dehydrogenase: its inhibition by H2-receptor antagonists, and its effect on the bioavailability of ethanol.
pubmed:affiliation
Alcohol Research and Treatment Center, Mount Sinai School of Medicine (CUNY), NY.
pubmed:publicationType
Journal Article, Comparative Study, Research Support, U.S. Gov't, P.H.S., Research Support, U.S. Gov't, Non-P.H.S.