| Literature DB >> 23125033 |
Amy J Claydon1, Robert Beynon.
Abstract
Although bulk protein turnover has been measured with the use of stable isotope labeled tracers for over half a century, it is only recently that the same approach has become applicable to the level of the proteome, permitting analysis of the turnover of many proteins instead of single proteins or an aggregated protein pool. The optimal experimental design for turnover studies is dependent on the nature of the biological system under study, which dictates the choice of precursor label, protein pool sampling strategy, and treatment of data. In this review we discuss different approaches and, in particular, explore how complexity in experimental design and data processing increases as we shift from unicellular to multicellular systems, in particular animals.Mesh:
Substances:
Year: 2012 PMID: 23125033 PMCID: PMC3518130 DOI: 10.1074/mcp.O112.022186
Source DB: PubMed Journal: Mol Cell Proteomics ISSN: 1535-9476 Impact factor: 5.911