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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
20
|
| pubmed:dateCreated |
1987-8-13
|
| pubmed:abstractText |
Interaction between the alpha-ketoglutarate dehydrogenase complex and NAD+-dependent isocitrate dehydrogenase was detected with a variety of techniques including polyethylene glycol precipitation, ultracentrifugation, and centrifugal gel filtration on a Sepharose 6B column. The interaction was specific in that citrate synthase, cytosolic malate dehydrogenase, and NADP-dependent isocitrate dehydrogenase did not interact with alpha-ketoglutarate dehydrogenase complex. The interaction was not inhibited by either 0.1 M KCl or 0.4 M (NH4)2SO4, but was completely prevented by 5% glycerol. A new method for the preparation of NADH: ubiquinone oxidoreductase resulted in an enzyme having a protein subunit composition similar to that of classical complex I preparation. Evidence is given for the existence of ternary complexes containing NADH:ubiquinone oxidoreductase-alpha-ketoglutarate dehydrogenase complex-NAD-dependent isocitrate dehydrogenase and NADH: ubiquinone oxidoreductase-alpha-ketoglutarate dehydrogenase complex-succinate thiokinase. These data suggest that a part of the citric acid cycle may be located in the vicinity of NADH: ubiquinone oxidoreductase. These complexes may facilitate the transport of metabolites among these enzymes without their equilibrating with the whole compartment.
|
| pubmed:language |
eng
|
| pubmed:journal | |
| pubmed:citationSubset |
IM
|
| pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Isocitrate Dehydrogenase,
http://linkedlifedata.com/resource/pubmed/chemical/Ketoglutarate Dehydrogenase Complex,
http://linkedlifedata.com/resource/pubmed/chemical/Ketone Oxidoreductases,
http://linkedlifedata.com/resource/pubmed/chemical/Malate Dehydrogenase,
http://linkedlifedata.com/resource/pubmed/chemical/NAD(P)H Dehydrogenase (Quinone),
http://linkedlifedata.com/resource/pubmed/chemical/Quinone Reductases
|
| pubmed:status |
MEDLINE
|
| pubmed:month |
Jul
|
| pubmed:issn |
0021-9258
|
| pubmed:author | |
| pubmed:issnType |
Print
|
| pubmed:day |
15
|
| pubmed:volume |
262
|
| pubmed:owner |
NLM
|
| pubmed:authorsComplete |
Y
|
| pubmed:pagination |
9509-14
|
| pubmed:dateRevised |
2007-11-15
|
| pubmed:meshHeading |
pubmed-meshheading:3110160-Cytosol,
pubmed-meshheading:3110160-Electrophoresis, Polyacrylamide Gel,
pubmed-meshheading:3110160-Isocitrate Dehydrogenase,
pubmed-meshheading:3110160-Ketoglutarate Dehydrogenase Complex,
pubmed-meshheading:3110160-Ketone Oxidoreductases,
pubmed-meshheading:3110160-Kinetics,
pubmed-meshheading:3110160-Malate Dehydrogenase,
pubmed-meshheading:3110160-Molecular Weight,
pubmed-meshheading:3110160-NAD(P)H Dehydrogenase (Quinone),
pubmed-meshheading:3110160-Quinone Reductases
|
| pubmed:year |
1987
|
| pubmed:articleTitle |
Interaction between NAD-dependent isocitrate dehydrogenase, alpha-ketoglutarate dehydrogenase complex, and NADH:ubiquinone oxidoreductase.
|
| pubmed:publicationType |
Journal Article
|