| pubmed-article:4083900 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:4083900 | lifeskim:mentions | umls-concept:C1882726 | lld:lifeskim |
| pubmed-article:4083900 | lifeskim:mentions | umls-concept:C0030016 | lld:lifeskim |
| pubmed-article:4083900 | lifeskim:mentions | umls-concept:C0205463 | lld:lifeskim |
| pubmed-article:4083900 | lifeskim:mentions | umls-concept:C1511539 | lld:lifeskim |
| pubmed-article:4083900 | lifeskim:mentions | umls-concept:C0851285 | lld:lifeskim |
| pubmed-article:4083900 | pubmed:issue | 2 | lld:pubmed |
| pubmed-article:4083900 | pubmed:dateCreated | 1986-1-30 | lld:pubmed |
| pubmed-article:4083900 | pubmed:abstractText | A radiochemical assay was developed for measuring branched-chain alpha-ketoacid dehydrogenase activity of Triton X-100 extracts of freeze-clamped rat liver. The proportion of active (dephosphorylated) enzyme was determined by measuring enzyme activities before and after activation of the complex with a broad-specificity phosphoprotein phosphatase. Hepatic branched-chain alpha-ketoacid dehydrogenase activity in normal male Wistar rats was 97% active but decreased to 33% active after 2 days on low-protein (8%) diet and to 13% active after 4 days on the same diet. Restricting protein intake of lean and obese female Zucker rats also caused inactivation of hepatic branched-chain alpha-ketoacid dehydrogenase complex. Essentially all of the enzyme was in the active state in rats maintained for 14 days on either 30 or 50% protein diets. This was also the case for rats maintained on a commercial chow diet (minimum 23% protein). However, maintaining rats on 20, 8, and 0% protein diets decreased the percentage of the active form of the enzyme to 58, 10, and 7% of the total, respectively. Fasting of chow-fed rats for 48 h had no effect on the activity state of hepatic branched-chain alpha-ketoacid dehydrogenase, i.e., 93% of the enzyme remained in the active state compared to 97% for chow-fed rats. However, hepatic enzyme of rats maintained on 8% protein diet was 10% active before starvation and 83% active after 2 days of starvation. Thus, dietary protein deficiency results in inactivation of hepatic branched-chain alpha-ketoacid dehydrogenase complex, presumably as a consequence of low hepatic levels of branched-chain alpha-ketoacids, established inhibitors of branched-chain alpha-ketoacid dehydrogenase kinase. With rats fed a low-protein diet and subsequently starved, inhibition of branched-chain alpha-ketoacid dehydrogenase kinase by branched-chain alpha-ketoacids generated as a consequence of endogenous proteolysis most likely promotes the greater branched-chain alpha-ketoacid dehydrogenase activity state. | lld:pubmed |
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| pubmed-article:4083900 | pubmed:language | eng | lld:pubmed |
| pubmed-article:4083900 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:4083900 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:4083900 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:4083900 | pubmed:month | Dec | lld:pubmed |
| pubmed-article:4083900 | pubmed:issn | 0003-9861 | lld:pubmed |
| pubmed-article:4083900 | pubmed:author | pubmed-author:HarrisR ARA | lld:pubmed |
| pubmed-article:4083900 | pubmed:author | pubmed-author:PowellS MSM | lld:pubmed |
| pubmed-article:4083900 | pubmed:author | pubmed-author:PaxtonRR | lld:pubmed |
| pubmed-article:4083900 | pubmed:author | pubmed-author:NagaeHH | lld:pubmed |
| pubmed-article:4083900 | pubmed:author | pubmed-author:GillimS ESE | lld:pubmed |
| pubmed-article:4083900 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:4083900 | pubmed:volume | 243 | lld:pubmed |
| pubmed-article:4083900 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:4083900 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:4083900 | pubmed:pagination | 542-55 | lld:pubmed |
| pubmed-article:4083900 | pubmed:dateRevised | 2007-11-14 | lld:pubmed |
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| pubmed-article:4083900 | pubmed:year | 1985 | lld:pubmed |
| pubmed-article:4083900 | pubmed:articleTitle | Physiological covalent regulation of rat liver branched-chain alpha-ketoacid dehydrogenase. | lld:pubmed |
| pubmed-article:4083900 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:4083900 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:4083900 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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