A comparison of methods for the measurement of protein turnover in vivo
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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.
1980 ◽
Vol 238
(1)
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pp. E46-E52
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2013 ◽
Vol 304
(8)
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pp. E895-E907
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1980 ◽
Vol 44
(2)
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pp. 129-140
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1986 ◽
Vol 250
(2)
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pp. E114-E120
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1997 ◽
Vol 273
(6)
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pp. E1149-E1157
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2009 ◽
Vol 106
(5)
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pp. 1692-1701
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