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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
1
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pubmed:dateCreated |
1982-1-20
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pubmed:abstractText |
1. Pig heart pyruvate dehydrogenase phosphate complex in which all three sites of phosphorylation were completely phosphorylated was re-activated at a slower rate by phosphatase than complex predominantly phosphorylated in site 1. The ratio of initial rates of re-activation was approx. 1:5 with a comparatively crude preparation of phosphatase and with phosphatase purified by gel filtration and ion-exchange chromatography. 2. The ratio of apparent first-order rate constants during dephosphorylation of fully phosphorylated complex averaged 1/3.8/1.3 for site 1/site 2/site 3. Only site-1 dephosphorylation was linearly correlated with re-activation of the complex throughout dephosphorylation. Dephosphorylation of site 3 was linearly correlated with re-activation after an initial burst of dephosphorylation. 3. Because dephosphorylation of site 1 was always associated with dephosphorylation of site 2, it is concluded that dephosphorylation cannot be purely random. 4. The ratio of apparent first-order rate constants for dephosphorylation of site 1 (partially/fully phosphorylated complexes) averaged 1.72. This ratio is smaller than the ratio of approx. 5 for the initial rates of re-activation. Possible mechanisms involved in the diminished rate of re-activation of fully phosphorylated complex are discussed.
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/6272748-180974,
http://linkedlifedata.com/resource/pubmed/commentcorrection/6272748-191033,
http://linkedlifedata.com/resource/pubmed/commentcorrection/6272748-204298,
http://linkedlifedata.com/resource/pubmed/commentcorrection/6272748-212016,
http://linkedlifedata.com/resource/pubmed/commentcorrection/6272748-227365,
http://linkedlifedata.com/resource/pubmed/commentcorrection/6272748-230091,
http://linkedlifedata.com/resource/pubmed/commentcorrection/6272748-4306045,
http://linkedlifedata.com/resource/pubmed/commentcorrection/6272748-4339646,
http://linkedlifedata.com/resource/pubmed/commentcorrection/6272748-4375962,
http://linkedlifedata.com/resource/pubmed/commentcorrection/6272748-454401,
http://linkedlifedata.com/resource/pubmed/commentcorrection/6272748-496891,
http://linkedlifedata.com/resource/pubmed/commentcorrection/6272748-6018,
http://linkedlifedata.com/resource/pubmed/commentcorrection/6272748-6244187,
http://linkedlifedata.com/resource/pubmed/commentcorrection/6272748-678513,
http://linkedlifedata.com/resource/pubmed/commentcorrection/6272748-6892624,
http://linkedlifedata.com/resource/pubmed/commentcorrection/6272748-697742,
http://linkedlifedata.com/resource/pubmed/commentcorrection/6272748-7305968,
http://linkedlifedata.com/resource/pubmed/commentcorrection/6272748-7396870
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Apr
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pubmed:issn |
0264-6021
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
1
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pubmed:volume |
195
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
51-9
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pubmed:dateRevised |
2009-11-18
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pubmed:meshHeading |
pubmed-meshheading:6272748-Animals,
pubmed-meshheading:6272748-Binding Sites,
pubmed-meshheading:6272748-Enzyme Activation,
pubmed-meshheading:6272748-Kinetics,
pubmed-meshheading:6272748-Myocardium,
pubmed-meshheading:6272748-Phosphopeptides,
pubmed-meshheading:6272748-Phosphoprotein Phosphatases,
pubmed-meshheading:6272748-Phosphorylation,
pubmed-meshheading:6272748-Pyruvate Dehydrogenase (Lipoamide)-Phosphatase,
pubmed-meshheading:6272748-Pyruvate Dehydrogenase Complex,
pubmed-meshheading:6272748-Swine,
pubmed-meshheading:6272748-Thermolysin
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pubmed:year |
1981
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pubmed:articleTitle |
Dephosphorylation of pig heart pyruvate dehydrogenase phosphate complexes by pig heart pyruvate dehydrogenase phosphate phosphatase.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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