Linked Life Data

3420620

Source:http://linkedlifedata.com/resource/pubmed/id/3420620

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
1988-10-27
pubmed:abstractText
The substrate preference of an aldehyde dehydrogenase induced in rat liver cytosol by 3-methylcholanthrene was examined. This enzyme, T-ALDH, is identical to the aldehyde dehydrogenase inducible in rat liver by 2,3,7,8-tetrachloro-dibenzo-p-dioxin and the tumor-associated aldehyde dehydrogenase found in rat hepatocellular neoplasms. With either NAD or NADP as coenzyme, the preferred substrates were the aliphatic aldehydes n-hexanal, n-nonanal, and isobutyraldehyde and the aromatic aldehydes 2,5-dihydroxybenzaldehyde, benzaldehyde, and 3-hydroxybenzaldehyde. The results indicate that T-ALDH may play a role in oxidizing a variety of aldehydes produced in physiological lipid metabolism. On the contrary, this isozyme does not seem to participate in the oxidation of small aliphatic aldehydes generated during lipid peroxidation. Similarly, no significant activity could be detected when the enzyme was tested with aldehydes produced in carbohydrate, amino acid, polyamine, steroid, and vitamin metabolism.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Sep
pubmed:issn
0041-008X
pubmed:author
pubmed:issnType
Print
pubmed:day
15
pubmed:volume
95
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
339-45
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed:year
1988
pubmed:articleTitle
Substrate preference of a cytosolic aldehyde dehydrogenase inducible in rat liver by treatment with 3-methylcholanthrene.
pubmed:affiliation
Department of Pharmacology, Medical School, University of Ioannina, Greece.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S.