pubmed-article:6272748 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:6272748 | lifeskim:mentions | umls-concept:C0039005 | lld:lifeskim |
pubmed-article:6272748 | lifeskim:mentions | umls-concept:C0018787 | lld:lifeskim |
pubmed-article:6272748 | lifeskim:mentions | umls-concept:C0031603 | lld:lifeskim |
pubmed-article:6272748 | lifeskim:mentions | umls-concept:C0034346 | lld:lifeskim |
pubmed-article:6272748 | lifeskim:mentions | umls-concept:C1158884 | lld:lifeskim |
pubmed-article:6272748 | lifeskim:mentions | umls-concept:C0034343 | lld:lifeskim |
pubmed-article:6272748 | lifeskim:mentions | umls-concept:C1704241 | lld:lifeskim |
pubmed-article:6272748 | pubmed:issue | 1 | lld:pubmed |
pubmed-article:6272748 | pubmed:dateCreated | 1982-1-20 | lld:pubmed |
pubmed-article:6272748 | 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. | lld:pubmed |
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pubmed-article:6272748 | pubmed:language | eng | lld:pubmed |
pubmed-article:6272748 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:6272748 | pubmed:citationSubset | IM | lld:pubmed |
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pubmed-article:6272748 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:6272748 | pubmed:month | Apr | lld:pubmed |
pubmed-article:6272748 | pubmed:issn | 0264-6021 | lld:pubmed |
pubmed-article:6272748 | pubmed:author | pubmed-author:RandleP JPJ | lld:pubmed |
pubmed-article:6272748 | pubmed:author | pubmed-author:KerbeyA LAL | lld:pubmed |
pubmed-article:6272748 | pubmed:author | pubmed-author:KearnyGG | lld:pubmed |
pubmed-article:6272748 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:6272748 | pubmed:day | 1 | lld:pubmed |
pubmed-article:6272748 | pubmed:volume | 195 | lld:pubmed |
pubmed-article:6272748 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:6272748 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:6272748 | pubmed:pagination | 51-9 | lld:pubmed |
pubmed-article:6272748 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
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pubmed-article:6272748 | pubmed:year | 1981 | lld:pubmed |
pubmed-article:6272748 | pubmed:articleTitle | Dephosphorylation of pig heart pyruvate dehydrogenase phosphate complexes by pig heart pyruvate dehydrogenase phosphate phosphatase. | lld:pubmed |
pubmed-article:6272748 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:6272748 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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