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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Research Article| November 15 1979
A comparison of methods for the measurement of protein turnover in vivo
M L MacDonald;
S L Augustine;
Biochem J (1979) 184 (2): 473–476.
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M L MacDonald, S L Augustine, T L Burk, R W Swick; A comparison of methods for the measurement of protein turnover in vivo. Biochem J 15 November 1979; 184 (2): 473–476. doi: https://doi.org/10.1042/bj1840473
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