Zänglein N, Tucher J, Pischetsrieder M (2015)
Publication Type: Journal article
Publication year: 2015
Publisher: Elsevier
Book Volume: 117
Pages Range: 58-69
DOI: 10.1016/j.jprot.2015.01.010
Comprehensive physiological food assessment requires recording of activity profiles. To elucidate the nutritive regulation of antioxidant enzymes, a generally applicable targeted MS method was established for the expression analysis of catalase and then adapted to heme oxygenase-1. Before tryptic digestion, target proteins were prefractionated by off-gel IEF of stimulated and control cell lysate. Targeted proteome analysis was achieved by LC coupled with scheduled selected reaction monitoring MS using 2 proteotypic peptides per protein and 3-4 transitions per peptide. Relative quantification was performed by stable isotope labeling by amino acids in cell culture (SILAC). The assay showed good correlation with results by Western blot. Linearity, precision, and sensitivity were even improved (LC/SRM vs. Western blot: 3 vs. 1 orders of magnitude, RSD 3.7-13.7% vs. 18.4%, LOD 0.2 vs. 1.6μg/mL). The developed method indicated that coffee does not modulate catalase expression in macrophages (T7
APA:
Zänglein, N., Tucher, J., & Pischetsrieder, M. (2015). Targeted mass spectrometry for the analysis of nutritive modulation of catalase and heme oxygenase-1 expression. Journal of Proteomics, 117, 58-69. https://doi.org/10.1016/j.jprot.2015.01.010
MLA:
Zänglein, Nina, Joanna Tucher, and Monika Pischetsrieder. "Targeted mass spectrometry for the analysis of nutritive modulation of catalase and heme oxygenase-1 expression." Journal of Proteomics 117 (2015): 58-69.
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