A comparison of methods for the measurement of protein turnover in vivo
| Autor: | S L Augustine, M L MacDonald, R W Swick, T L Burk |
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| Rok vydání: | 1979 |
| Předmět: |
Male
History Continuous infusion Ornithine aminotransferase Bicarbonate Biology Tritium Education chemistry.chemical_compound In vivo Fructose-Bisphosphate Aldolase Methods Animals Carbon Radioisotopes Tyrosine HEPATIC PROTEIN chemistry.chemical_classification Ornithine-Oxo-Acid Transaminase Muscles Protein turnover Proteins Rats Computer Science Applications Amino acid Bicarbonates Kinetics Liver chemistry Biochemistry Research Article |
| Zdroj: | Biochemical Journal. 184:473-476 |
| ISSN: | 0306-3283 |
| DOI: | 10.1042/bj1840473 |
| Popis: | 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. |
| Databáze: | OpenAIRE |
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