| Range |
mean 0.081h^-1: median 0.034h^-1 hours^-1
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| Organism |
Human Homo sapiens |
| Reference |
Doherty MK, Hammond DE, Clague MJ, Gaskell SJ, Beynon RJ. Turnover of the human proteome: determination of protein intracellular stability by dynamic SILAC. J Proteome Res. 2009 Jan8(1):104-12. doi: 10.1021/pr800641v. p.106 right column top paragraphPubMed ID18954100
|
| Method |
Abstract:"In this work, [investigators] have analyzed time-dependent changes in the incorporation of a stable amino acid resolved precursor, a protocol [they] refer to as "dynamic SILAC", using 1-D gel separation followed by in-gel digestion and LC-MS/MS [Liquid chromatography–mass spectrometry] analyses to profile the intracellular stability of almost 600 proteins from human A549 adenocarcinoma cells, requiring multiple measures of the extent of labeling with stable isotope labeled amino acids in a classic label-chase experiment." |
| Comments |
P.106 left column bottom of column:"The calculated degradation rates ranged from 2×10^−5±9×10−^07h^−1 to 5.4±0.4h^−1, relating to half-lives of many tens of hours to just 6 min. For the 576 nonredundant values, the mean degradation rate was 0.081h^−1 and the median degradation rate was 0.034h^−1. The degradation rate constants were not normally distributed (Kolmogorov−Smirnov test, P < 0.001), and although the data could be log-transformed to normality, all statistical analyses have been conducted on untransformed data using nonparametric methods. Although these data generate absolute turnover rates, they cannot be extrapolated to other cell types or tissues without a degree of caution (refs 4, 5) and are of greatest value in internal analyses of factors that modulate protein stability." |
| Entered by |
Uri M |
| ID |
112253 |