Cold storage is being used to increase nectarine fruits' postharvest life. However, low temperatures lead to chilling injury and limit their commercial quality and value. In this study a proteomic approach was used to compare the protein profile between control and cold storage nectarine fruits. Protein extracted from tissue was resolved by two-dimensional gel electrophoresis (2-DE) in the 4-7 pH and 10-200 kDa Mr range. Around 350 spots were well determined, and 11 from 17 spots that showed significant differences were identified by peptide mass fingerprinting (PMF) using matrix-assisted laser desorption/ionization (MALDI)-time-of-flight (TOF)-mass spectrometry (MS). Four differentially expressed proteins were characterized as allergens and were further assessed at the transcription level using quantitative real time-RT-PCR (qRT-PCR).
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