Proteome changes in bovine longissimus thoracis muscle during the early postmortem storage period.
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.
Jia
Xiaohong
X
Matforsk AS, Norwegian Food Research Institute, Osloveien 1, N-1430 As, Norway.
Ekman
Maria
M
Grove
Harald
H
Faergestad
Ellen M
EM
Aass
Laila
L
Hildrum
Kjell I
KI
Hollung
Kristin
K
D000818:Animals; D002417:Cattle; D015180:Electrophoresis, Gel, Two-Dimensional; D008460:Meat; D009124:Muscle Proteins / Q000032:analysis*; D018482:Muscle, Skeletal / Q000737:chemistry*; D011180:Postmortem Changes; D020543:Proteome / Q000032:analysis*; D040901:Proteomics; D019032:Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization
D009124:Muscle Proteins; D020543:Proteome