Linked Life Data

3790167

Source:http://linkedlifedata.com/resource/pubmed/id/3790167

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
24
pubmed:dateCreated
1987-1-14
pubmed:abstractText
Pathways of ethanol elimination in alcohol dehydrogenase (ADH)-positive and -negative deermice were studied using the catalase inhibitor, 3-amino-1,2,4-triazole. To verify that aminotriazole inhibited catalase effectively, the characteristic decrease in catalase-H2O2 which occurs in saline-treated controls when ethanol is peroxidized was monitored at 660-640 nm in perfused deermouse livers. Following 1.5 hr of pretreatment with aminotriazole (1.5 g/kg), the peroxidatic activity of catalase measured in vitro was inhibited by greater than 99%. Under these conditions, ethanol did not decrease catalase-H2O2 in perfused livers, indicating that catalase was inhibited. Ethanol and aniline oxidation by microsomes were also inhibited by about 67-90% after 1.5 hr of pretreatment with aminotriazole. In ADH-positive deermice, pretreatment with aminotriazole for 1.5 hr prior to injection of ethanol (2.0 g/kg) decreased rates of ethanol elimination in vivo from 13.2 +/- 0.8 to 10.2 +/- 0.4 mmoles/kg/hr. In ADH-negative deermice, similar treatment decreased rates of ethanol elimination in vivo from 4.5 +/- 0.4 to 1.1 +/- 0.6 mmoles/kg/hr. Following pretreatment with aminotriazole (1.0 g/kg) for 6 hr, rates of ethanol elimination in ADH-negative deermice returned to near basal values. Under these conditions, the peroxidatic activity of catalase measured in vitro and the ethanol-dependent decrease in catalase-H2O2 in perfused livers also returned to near basal levels; however, the oxidation of ethanol by cytochrome P-450 was inhibited completely. It is concluded, therefore, that time of pretreatment with aminotriazole is an important variable which must be controlled carefully to inhibit catalase completely. Since catalase was active while cytochrome P-450 was not following 6 hr of pretreatment with aminotriazole, it is concluded that ethanol elimination occurs predominantly via catalase-H2O2 in ADH-negative deermice under these conditions.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Dec
pubmed:issn
0006-2952
pubmed:author
pubmed:issnType
Print
pubmed:day
15
pubmed:volume
35
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
4487-92
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed:year
1986
pubmed:articleTitle
Catalase-dependent ethanol metabolism in vivo in deermice lacking alcohol dehydrogenase.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't