期刊
JOURNAL OF PROTEOMICS
卷 75, 期 9, 页码 2660-2669出版社
ELSEVIER
DOI: 10.1016/j.jprot.2012.03.020
关键词
Selected reaction monitoring; Mass spectrometry; Protein quantification; Acetate metabolism
资金
- Bundesministerium fur Bildung und Forschung (BMBF) [0316017B]
Selected reaction monitoring allows quantitative measurements of proteins over several orders of magnitude in complex biological samples. Here we present a targeted approach for quantification of 19 enzymes from Corynebacterium glutamicum applying isotope dilution mass spectrometry coupled to high performance liquid chromatography (IDMS-LC-MS/MS). Investigations of protein dynamics upon growth on acetate and glucose as sole carbon source shows highly stable peptide amounts for enzymes of the central carbon metabolism during the transition phase and after substrate depletion. However significant adaptations of protein amounts are observed between both growth conditions well agreeing with known changes in metabolic fluxes. Time-resolved measurements of protein expression after metabolic switch from glycolytic to gluconeogenetic conditions reveal fast responses in protein synthesis rates for glyoxylate shunt enzymes. (C) 2012 Elsevier B.V. All rights reserved.
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