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Properties of 13C-Substituted Arginine in Stable Isotope Labeling by Amino Acids in Cell Culture (SILAC)
Abstract
We have recently described a method, stable isotope labeling by amino acids in cell culture (SILAC) for the accurate quantitation of relative protein abundances. Cells were metabolically labeled with deuterated leucine, leading to complete incorporation within about five cell doublings. Here, we investigate fully substituted 13C-labeled arginine in the SILAC method. After tryptic digestion, there is a single label at the C-terminal position in half of the peptides. Labeled and unlabeled peptides coelute in liquid chromatography-mass spectrometric analysis, eliminating quantitation error due to unequal sampling of ion profiles. Tandem mass spectrum interpretation and database identification are aided by the predictable shift of the y-ions in the labeled form. The quantitation of mixtures of total cell lysates in known ratios resolved on a one-dimensional SDS-PAGE gel produced consistent and reproducible results with relative standard deviations better than five percent under optimal conditions.
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“Stable isotope labeling with amino acids in cell culture (SILAC, Ong et al., 2002, 2003) was achieved by propagating cells in RPMI 1640 free of L-lysine, L-arginine and L-glutamine (PAA Laboratories) supplemented with 220 µM L-lysine and 144 µM L-arginine in either their light (Lys-0 and Arg-0) or…”
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Metadata
- Authors
- Ong, S.-E., Kratchmarova, I., & Mann, M.
- Venue
- Journal of Proteome Research
- Publisher
- American Chemical Society (ACS)
- Published
- 2002-12-13
- Volume
- 2
- Issue
- 2
- Pages
- 173-181
- ISSN
- 1535-3893 (ISSN-L)
- 1535-3907
- OpenAlex
- W2064543105
- Cited by
- 432
- References
- 0
- FWCI
- 8.09
- Type
- journal article
- Language
- en
- Open access
- closed
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