Linked Life Data

9851831

Source:http://linkedlifedata.com/resource/pubmed/id/9851831

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
1999-1-20
pubmed:abstractText
At pH 7.05 NADH-X prepared by incubating NADH with glyceraldehyde-3-phosphate dehydrogenase (E.C. 1.2.1.12) was a potent noncompetitive inhibitor, with respect to coenzyme, of NADPH oxidation by pure rabbit muscle cytosolic glycerol-3-phosphate dehydrogenase (E.C. 1.1.1.8) and also a potent inhibitor of NADPH oxidation catalyzed by this enzyme in a rat pancreatic islet cytosolic fraction. It was a much less potent inhibitor of NADPH oxidation catalyzed by this enzyme in a rat liver cytosolic fraction and of NADH oxidation catalyzed by this enzyme from all three sources. Glycerol-3-phosphate dehydrogenase purified from muscle cytosol contains tightly bound NADH-X, NAD, and ADP-ribose, each in amounts of about 0.1 mol per mole of enzyme polypeptide chain. A deproteinized supernatant of this enzyme contained these three ligands and produced the same type of inhibition of the enzyme described above for prepared NADH-X with a Ki, in the reaction with NADPH at pH 7.05, in the range of 0.2 microM with respect to the total concentration of ligands ([ADP-ribose] + [NAD] + [NADH-X] = 0. 2 microM). However, only the NADH-X component could account for the potent inhibition because NAD, ADP-ribose, and the primary acid product (which can be produced from NADH-X) each had a Ki considerably higher than 0.2 microM. Although at pH 7.05 NADH-X inhibited NADPH oxidation considerably more than NADH oxidation, the reverse was the case at pH 7.38. Since the enzyme purified from muscle contains tightly bound NADH-X, NADH-X might become attached to the enzyme in vivo where it could play a role in regulating the ratio of NADH to NADPH oxidation of the enzyme.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Dec
pubmed:issn
0003-9861
pubmed:author
pubmed:copyrightInfo
Copyright 1998 Academic Press.
pubmed:issnType
Print
pubmed:day
15
pubmed:volume
360
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
195-205
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed-meshheading:9851831-Adenosine Diphosphate Ribose, pubmed-meshheading:9851831-Animals, pubmed-meshheading:9851831-Chromatography, High Pressure Liquid, pubmed-meshheading:9851831-Cytosol, pubmed-meshheading:9851831-Dialysis, pubmed-meshheading:9851831-Enzyme Activation, pubmed-meshheading:9851831-Glyceraldehyde-3-Phosphate Dehydrogenases, pubmed-meshheading:9851831-Glycerol-3-Phosphate Dehydrogenase (NAD+), pubmed-meshheading:9851831-Glycerolphosphate Dehydrogenase, pubmed-meshheading:9851831-Hydrogen-Ion Concentration, pubmed-meshheading:9851831-Islets of Langerhans, pubmed-meshheading:9851831-Kinetics, pubmed-meshheading:9851831-Ligands, pubmed-meshheading:9851831-Liver, pubmed-meshheading:9851831-Muscle, Skeletal, pubmed-meshheading:9851831-NAD, pubmed-meshheading:9851831-NADP, pubmed-meshheading:9851831-Oxidation-Reduction, pubmed-meshheading:9851831-Rabbits, pubmed-meshheading:9851831-Rats
pubmed:year
1998
pubmed:articleTitle
Effect of NADH-X on cytosolic glycerol-3-phosphate dehydrogenase.
pubmed:affiliation
Department of Pharmacology, Department of Pediatrics, University of Wisconsin Medical School, 1330 University Avenue, Madison, Wisconsin, 53706, USA.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S.