Linked Life Data

2509445

Source:http://linkedlifedata.com/resource/pubmed/id/2509445

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
30
pubmed:dateCreated
1989-11-27
pubmed:abstractText
Bovine lens aldose reductase (alditol:NADP+ oxidoreductase, EC 1.1.1.21) undergoes an oxidative modification, greatly stimulated by high ionic strength, upon incubation in the presence of oxygen radical generating systems (Del Corso, A., Camici, M., and Mura, U. (1987) Biochem. Biophys. Res. Commun. 148, 369-375). The enzyme modification is accompanied by a change in stereospecificity toward the two enantiomers of glyceraldehyde. In particular, the Km for L-glyceraldehyde of the native form increased over 150 times after the enzyme modification, with a decrease in the catalytic efficiency of over 200 times. By contrast, for the D-enantiomer the Km increased only 7 times with respect to the native form, with a concomitant decrease in the catalytic efficiency of only approximately 3 times. This dramatic change in stereospecificity may account for the reported apparent cooperative behavior exhibited also by highly purified electrophoretically homogeneous preparations of aldose reductase.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Oct
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
25
pubmed:volume
264
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
17653-5
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1989
pubmed:articleTitle
Change in stereospecificity of bovine lens aldose reductase modified by oxidative stress.
pubmed:affiliation
Department of Physiology, University of Pisa, Italy.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't