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Mol Cell Proteomics. 2014 May;13(5):1352-8. doi: 10.1074/mcp.M113.031914. Epub 2014 Feb 21.

Quantitative, time-resolved proteomic analysis by combining bioorthogonal noncanonical amino acid tagging and pulsed stable isotope labeling by amino acids in cell culture.

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1
Division of Chemistry and Chemical Engineering, California Institute of Technology, Pasadena, California;

Abstract

An approach to proteomic analysis that combines bioorthogonal noncanonical amino acid tagging (BONCAT) and pulsed stable isotope labeling with amino acids in cell culture (pSILAC) provides accurate quantitative information about rates of cellular protein synthesis on time scales of minutes. The method is capable of quantifying 1400 proteins produced by HeLa cells during a 30 min interval, a time scale that is inaccessible to isotope labeling techniques alone. Potential artifacts in protein quantification can be reduced to insignificant levels by limiting the extent of noncanonical amino acid tagging. We find no evidence for artifacts in protein identification in experiments that combine the BONCAT and pSILAC methods.

PMID:
24563536
PMCID:
PMC4014290
DOI:
10.1074/mcp.M113.031914
[Indexed for MEDLINE]
Free PMC Article
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