Linked Life Data

7267735

Source:http://linkedlifedata.com/resource/pubmed/id/7267735

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
6
pubmed:dateCreated
1981-10-14
pubmed:abstractText
Incubation of horse liver aldehyde dehydrogenase (aldehyde:NAD oxidoreductase, EC 1.2.1.3) with 2-hydroxyethyl disulfide formed mixed-disulfides between protein sulfhydryl groups and beta-mercaptoethanol. Reduction of aldehyde dehydrogenase activity may be associated with formation of one, or at most two, mixed-disulfides per dehydrogenase subunit. Characteristically in the case of a mixed-disulfide, inactivation was was reversed by addition of thiols. Other disulfides also inactivated aldehyde dehydrogenase. The pseudo first-order rate constants for the forward and reverse reactions (aldehyde dehydrogenase + 2-hydroxyethyl disulfide in equilibrium or formed from modified aldehyde dehydrogenase + beta-mercaptoethanol) were 0.70 and 2 liter mole-1 sec-1, respectively. The equilibrium constant was approximately 0.4. After extended incubation under conditions expected to result in complete modification of aldehyde dehydrogenase, 30% of the initial catalytic activity remained. This suggests that 2-hydroxyethyl disulfide-treated aldehyde dehydrogenase retains catalytic activity and that the sulfhydryl group modified by 2-hydroxyethyl disulfide is not essential for aldehyde dehydrogenase activity.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:issn
0031-9325
pubmed:author
pubmed:issnType
Print
pubmed:volume
12
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
483-95
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed:year
1980
pubmed:articleTitle
Reversible inactivation of horse liver aldehyde dehydrogenase by 2-hydroxyethyl disulfide.
pubmed:publicationType
Journal Article, Comparative Study, In Vitro, Research Support, U.S. Gov't, P.H.S., Research Support, U.S. Gov't, Non-P.H.S.