Linked Life Data

6127687

Source:http://linkedlifedata.com/resource/pubmed/id/6127687

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1196
pubmed:dateCreated
1982-12-21
pubmed:abstractText
The kinetics of dissociation of NADPH from its complex with isocitrate dehydrogenase, and from the abortive complex of enzyme, Mg2+, isocitrate and NADPH, have been studied in phosphate and triethanolamine buffers by means of rapid fluorescence measurements. The reactions are complex, and it is suggested that a conformational equilibrium of each of the complexes is involved, and that this conformational change is also responsible for a slow approach to the steady-state rate of oxidative decarboxylation observed previously in triethanolamine buffer under certain conditions (K. Dalziel, N. McFerran, B. Matthews & C.H. Reynolds, Biochem. J. 171, 743-750 (1978) ). It is concluded that release of free NADPH product is not the rate-limiting step in oxidative decarboxylation in the steady state. The validity of the ligand displacement method used to measure the dissociation kinetics of the enzyme-NADPH complex has been studied by computer simulation.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Feb
pubmed:issn
0080-4649
pubmed:author
pubmed:issnType
Print
pubmed:day
22
pubmed:volume
214
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
369-87
pubmed:dateRevised
2007-4-30
pubmed:meshHeading
pubmed:year
1982
pubmed:articleTitle
On the mechanism of NADP+-linked isocitrate dehydrogenase from heart mitochondria. I. The kinetics of dissociation of NADPH from its enzyme complex.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't