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• W2332877978 abstract "Cold-induced sweetening in potato tubers is a costly problem for the food industry. To systematically identify the proteins associated with this process, we employed a comparative proteomics approach using isobaric, stable isotope coded labels to compare the proteomes of potato tubers after 0 and 5 months of storage at 5 °C. We evaluated both high pH reverse phase (hpRP) liquid chromatography (LC) and off-gel electrophoresis (OGE) as first dimension fractionation methods followed by nanoLC–MS/MS, using two high performance mass spectrometry platforms (Q-TOF and Orbitrap). We found that hpRP-LC consistently offered better resolution, reduced expression ratio compression, and a more MS-compatible workflow than OGE and consistently yielded more unique peptide/protein identifications and higher sequence coverage with better quantification. In this study, a total of 4463 potato proteins were identified, of which 46 showed differential expressions during potato tuber cold storage. Several key proteins important in controlling starch–sugar conversion, which leads to cold-induced sweetening, as well as other proteins that are potentially involved in this process, were identified. Our results suggest that the hpRP-RP shotgun approach is a feasible and practical workflow for discovering potential protein candidates in plant proteomic analysis." @default.
• W2332877978 created "2016-06-24" @default.
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• W2332877978 date "2011-09-06" @default.
• W2332877978 modified "2023-10-14" @default.
• W2332877978 title "Evaluation of Different Multidimensional LC–MS/MS Pipelines for Isobaric Tags for Relative and Absolute Quantitation (iTRAQ)-Based Proteomic Analysis of Potato Tubers in Response to Cold Storage" @default.
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• W2332877978 doi "https://doi.org/10.1021/pr200455s" @default.
• W2332877978 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/21842911" @default.
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