Journal of Proteome Research · 2007 · 134 citations · 23 references
Life SciencesAnimal SciencesBiochemistryMeat ScienceMetabolismProteomicsMass Spectrometry-based ProteomicsMeat CompositionMeat PreservationMeat QualityProtein DegradationGlycolytic PathwaysMaldi-tof Mass SpectrometryMeat ProteinsPostmortem InvestigationPostmortem Muscle ChangesPostmortem ProteolysisTwo-dimensional ElectrophoresisTwo-dimensional Gel Electrophoresis
Postmortem changes in protein composition up to 24 h in bovine longissimus thoracis muscle were investigated by two-dimensional gel electrophoresis and MALDI-TOF MS/MS. A total of 47 spots were significantly changed the first 24 h postmortem. The 39 identified proteins can be divided into five groups: metabolic enzymes, defense and stress proteins, structural proteins, proteolytic enzymes, and unclassified proteins. The identified metabolic enzymes are all associated with ATP-generating pathways, either the glycolytic pathway or energy metabolism. In addition, several defense and stress proteins were changed in abundance in this study. These findings contribute to a better understanding of the biochemical processes during postmortem storage of meat.
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Mass Spectrometric Sequencing of Proteins from Silver-Stained Polyacrylamide Gels
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