Linked Life Data

3426675

Source:http://linkedlifedata.com/resource/pubmed/id/3426675

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:dateCreated
1988-3-23
pubmed:abstractText
The kinetic characteristics of alcohol dehydrogenase class III have been studied using class III isoenzymes purified from human liver (X-ADH) and rat liver (ADH-2). Our results confirm that long chain primary alcohols and aldehydes are the best substrates, although some aromatic compounds can also be actively metabolized. Kinetic analysis suggests an ordered bibi mechanism for X-ADH. Ethanol can be oxidized by class III isoenzymes at high substrate concentration, but with a very slow rate. Thus, their contribution to physiological ethanol elimination is probably insignificant. The general properties of the class III isoenzymes isolated from different mammals by ourselves and other authors are discussed.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:issn
1358-6173
pubmed:author
pubmed:issnType
Print
pubmed:volume
1
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
169-73
pubmed:dateRevised
2008-2-26
pubmed:meshHeading
pubmed:year
1987
pubmed:articleTitle
Mammalian alcohol dehydrogenase: characteristics of class III isoenzymes.
pubmed:affiliation
Department de Bioquímica i Biologia Molecular, Facultat de Ciències, Universitat Autònoma de Barcelona, Spain.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't