Linked Life Data

8627510

Source:http://linkedlifedata.com/resource/pubmed/id/8627510

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
1996-6-27
pubmed:abstractText
To assess the contribution of cytochrome P450 (P450) to the microsomal ethanol oxidation system (MEOS) in humans, we examined ethanol oxidization activity in human hepatic microsomes and multiple forms of human hepatic P450s expressed in B-lymphoblastoid cells. Acetaldehyde produced by the MEOS was converted into a fluorescent derivate with cyclohexane-1,3-dione and analyzed by high-performance liquid chromatography using a fluorescence detector. The ethanol oxidation activity of seven forms of human P450s was investigated. P450s 2E1 and 1A2 formed acetaldehyde at high rates. In immunoinhibition studies, anti-P450 2E1 antibody inhibited the ethanol oxidation activity of human hepatic microsomes by 54%, and anti-P450 1A2 antibody inhibited ethanol oxidation activity by 21%. 7,8-Benzoflavone, an inhibitor of P450 1A forms, also inhibited this activity by 38%. The correlation of ethanol oxidation activity with the levels of immunoreactive P450 2E1 in individual human microsomes was highly significant (r = 0.91, P < .001), and the correlation of ethanol oxidation activity with the levels of P450 1A2 was also highly significant (r = 0.87, P < .001). The Km values of P450s 2E1 and 1A2 for ethanol oxidation were 16.5 and 23.6 mM, respectively. These results indicated that P450 2E1 was a major contributor to the MEOS in humans; however, P450 1A2 was considered to play an important role in the MEOS.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
May
pubmed:issn
0022-3565
pubmed:author
pubmed:issnType
Print
pubmed:volume
277
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1004-9
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1996
pubmed:articleTitle
Microsomal ethanol oxidizing system activity by human hepatic cytochrome P450s.
pubmed:affiliation
Department of Public Health, Osaka City University Medical School, Japan.
pubmed:publicationType
Journal Article