| pubmed-article:534542 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:534542 | lifeskim:mentions | umls-concept:C0025663 | lld:lifeskim |
| pubmed-article:534542 | lifeskim:mentions | umls-concept:C0242485 | lld:lifeskim |
| pubmed-article:534542 | lifeskim:mentions | umls-concept:C0597297 | lld:lifeskim |
| pubmed-article:534542 | lifeskim:mentions | umls-concept:C1707455 | lld:lifeskim |
| pubmed-article:534542 | lifeskim:mentions | umls-concept:C1515655 | lld:lifeskim |
| pubmed-article:534542 | pubmed:issue | 2 | lld:pubmed |
| pubmed-article:534542 | pubmed:dateCreated | 1980-3-24 | lld:pubmed |
| pubmed-article:534542 | pubmed:abstractText | Steady-state rates of turnover of two single proteins were measured in vivo by two independent methods. The fractional rate of synthesis of liver ornithine aminotransferase, measured by a continuous infusion of L-[2,6-3H]tyrosine, was 0.42 day-1, whereas in the same animals the fractional rate of degradation measured by loss of radioactivity from amino acids labelled via [14C]bicarbonate was 0.40 day-1. The agreement between methods confirms the reliability of each method for the study of hepatic protein turnover. In contrast, [14C]bicarbonate-labelled amino acids are extensively reutilized in muscle, and are therefore unsuitable for measuring rates of muscle protein breakdown. | lld:pubmed |
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| pubmed-article:534542 | pubmed:language | eng | lld:pubmed |
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| pubmed-article:534542 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:534542 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:534542 | pubmed:month | Nov | lld:pubmed |
| pubmed-article:534542 | pubmed:issn | 0264-6021 | lld:pubmed |
| pubmed-article:534542 | pubmed:author | pubmed-author:MacDonaldM... | lld:pubmed |
| pubmed-article:534542 | pubmed:author | pubmed-author:SwickR WRW | lld:pubmed |
| pubmed-article:534542 | pubmed:author | pubmed-author:BurkT LTL | lld:pubmed |
| pubmed-article:534542 | pubmed:author | pubmed-author:AugustineS... | lld:pubmed |
| pubmed-article:534542 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:534542 | pubmed:day | 15 | lld:pubmed |
| pubmed-article:534542 | pubmed:volume | 184 | lld:pubmed |
| pubmed-article:534542 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:534542 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:534542 | pubmed:pagination | 473-6 | lld:pubmed |
| pubmed-article:534542 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
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| pubmed-article:534542 | pubmed:year | 1979 | lld:pubmed |
| pubmed-article:534542 | pubmed:articleTitle | A comparison of methods for the measurement of protein turnover in vivo. | lld:pubmed |
| pubmed-article:534542 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:534542 | pubmed:publicationType | Comparative Study | lld:pubmed |
| pubmed-article:534542 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
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