in 40S ribosome (S15a 805hrs: S6 6hrs) in 60S ribosome (L23a 144hrs: L4 2.6hrs) hours
||Human Homo sapiens
||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.109 right column bottom paragraphPubMed ID18954100
||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."
||P.109 right column bottom paragraph:"[Investigators] identified 27 individual subunits from each of the 40S and 60S ribosome and have measured the degradation rate of each (Figure 6). It is evident that the subunits do not turn over at a uniform rate. In the 40S ribosome, the S15a subunit was most stable with a kdeg of 0.0009 h^−1 (half-life = 805 h), whereas the S6 subunit has a kdeg of 0.11 h^−1 (half-life = 6 h), two orders of magnitude difference in stability. Similarly, the degradation rates of the 60S ribosome range from 0.0048 h^−1 (L23a, half-life = 144 h) to 0.031 h^−1 (L4, half-life = 2.6 h)."