Linked Life Data

9369240

Source:http://linkedlifedata.com/resource/pubmed/id/9369240

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
1997-12-4
pubmed:abstractText
Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) is a key glycolytic enzyme regulated by many diverse mechanisms. In this study we present evidence that GAPDH activity is stimulated in the presence of oxyhemoglobin (2.3-fold, P < 0.005). No stimulation was seen by myoglobin, and only slight stimulation (1.2-fold, not significant) by methemoglobin was observed. Such stimulation may have physiological significance as 1,3-bis-phosphoglycerate, the product of GAPDH, isomerises to 2,3-bis-phosphoglycerate, an allosteric effector that decreases the oxygen affinity of hemoglobin, thus providing a feedback loop. The results suggest that when assaying GAPDH activity in biological samples, hemoglobin content should be taken into account.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Oct
pubmed:issn
0014-5793
pubmed:author
pubmed:issnType
Print
pubmed:day
13
pubmed:volume
416
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
90-2
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1997
pubmed:articleTitle
Stimulation of glyceraldehyde-3-phosphate dehydrogenase by oxyhemoglobin.
pubmed:affiliation
Department of Neurochemistry, Institute of Neurology, London, UK. pbrookes@ion.ucl.ac.uk
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't