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Protein turnover analysis in metabolic labeling studies

Alexander Donald

The benefits of stable isotope labelling for proteomics have gradually come to light. However, a lot of stable isotope labelling techniques rely on labelling in vitro with intricate and occasionally pricey chemicals. The methodologies for labelling proteins in vivo through metabolic incorporation of labels into proteins are covered in this article. Although this method has several benefits and is particularly well adapted to single cells grown in culture (prokaryotic or eukaryotic), there are still a number of complicated elements that need to be controlled in order to conduct relevant studies. The metabolic instability of the precursor amino acid, insufficient labelling, and the impact of protein turnover on labelling kinetics are all confounding factors. If the proper safety measures are taken, all of these are manageable. This parameter's acquisition over a number of proteins enables comparisons between various tissues and the turnover profiling of cellular proteins. Muscle protein degrades on average at a far slower rate than liver or kidney, with the heart falling somewhere in the middle.