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. 1979 Nov 15;184(2):473–476. doi: 10.1042/bj1840473

A comparison of methods for the measurement of protein turnover in vivo.

M L MacDonald, S L Augustine, T L Burk, R W Swick
PMCID: PMC1161786  PMID: 534542

Abstract

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.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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