A sensitive method for measuring protein turnover based on the measurement of 2-3H-labelled amino acids in protein
- 15 June 1976
- journal article
- research article
- Published by Portland Press Ltd. in Biochemical Journal
- Vol. 156 (3), 561-568
- https://doi.org/10.1042/bj1560561
Abstract
A method for measuring the rate of protein degradation was described. The method measured the change in 2-3H content of protein with time by racemization of the protein hydrolysate with acetic anhydride. The 3H on C-2 of amino acids was stable in proteins but became labile, owing to the action of transaminases, once the amino acids were released by proteolysis. The specific measurement of 2-3H in amino acids largely overcame problems due to compartmentation and isotope recycling, and evidence to support this claim was presented. Values for the half-life of Lemna minor (duckweed) protein determined by the new method were compared with values obtained by other methods.This publication has 4 references indexed in Scilit:
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- D2O-Alanine exchange reactions catalyzed by Alanine Racemase and Glutamic Pyruvic TransaminaseBiochemical and Biophysical Research Communications, 1974
- Protein metabolism in cultured plant tissues. Calculation of an absolute rate of protein synthesis, accumulation, and degradation in tobacco callus in vivoBiochemistry, 1971
- The Turnover of Nucleic Acids in Lemna minorPlant Physiology, 1970