List of proteins examined and their turnover rate constants
Range | 0.05 - 0.20 Table - link 1/hour |
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Organism | Bacteria Streptomyces coelicolor |
Reference | Jayapal, K.P., Sui, S., Philp, R.J., Kok, Y.J., Yap, M.G., Griffin, T.J., and Hu, W.S. (2010) Multitagging proteomic strategy to estimate protein turnover rates in dynamic systems. J Proteome Res 9: 2087–2097. pp.2094-2095 table 1PubMed ID20184388 |
Method | "In an effort to segregate these two underlying mechanisms [protein synthesis and breakdown], a novel multitagging approach was developed based on stable isotope tagging (SILAC) and isobaric tag for relative and absolute quantification (iTRAQ) labelling." |
Comments | "Figure 6 shows the distribution of kmultitag values for 115 proteins quantified using SILAC-iTRAQ multitagging approach. The rate constants ranged from about 0.05 h^-1 to over 0.20 h^-1 for some proteins. The median value of kmultitag for the proteins was 0.097 h^-1 while the 25th and 75th percentile values were 0.081 h^-1 and 0.116 h^-1 respectively. This indicates that the majority of the proteins have kmultitag values ranging within a small interval with only a few proteins displaying very high or low rates of degradation. A list of these proteins, their kmultitag values, number of peptide hits and other relevant information are shown in Table 1." See notes beneath table |
Entered by | Uri M |
ID | 110439 |