Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
41
pubmed:dateCreated
1993-11-26
pubmed:abstractText
A modified Hummel-Dreyer equilibrium chromatography technique was used to test the hypothesis that NADH induces the molecular association of lactate dehydrogenase (LDH) and alpha-glycerol-3-phosphate dehydrogenase (alpha-GDH). In the presence of a very limited NADH concentration, a unique elution profile with a new peak running immediately ahead of a trough at the free alpha-GDH elution position is obtained. The appearance of this peak-trough profile is physical evidence that reversible association between LDH and alpha-GDH occurs over a very limited range of free NADH concentrations. The association constant for this complex formation between LDH and alpha-GDH is estimated to be 2.0 microM-1. With the NADH concentration increased to saturation level, no evidence of binding is observed. Such concentration-dependent behavior suggests that the strong competition between LDH and alpha-GDH for the limited amount of NADH tends to promote the enzyme-enzyme contact in order to make the most efficient use of the shared metabolite. The experimental results described in this article make a convincing argument for a metabolite-modulated enzyme-enzyme interaction along this metabolic pathway.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Oct
pubmed:issn
0006-2960
pubmed:author
pubmed:issnType
Print
pubmed:day
19
pubmed:volume
32
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
11124-31
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed:year
1993
pubmed:articleTitle
Metabolite-modulated complex formation between alpha-glycerophosphate dehydrogenase and lactate dehydrogenase.
pubmed:affiliation
Department of Chemistry, University of Oregon, Eugene 97403.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, U.S. Gov't, Non-P.H.S.