Journal
JOURNAL OF AGRICULTURAL AND FOOD CHEMISTRY
Volume 50, Issue 20, Pages 5508-5512Publisher
AMER CHEMICAL SOC
DOI: 10.1021/jf025555n
Keywords
porcine proteins; skeletal muscle proteins meat quality post mortem changes; protein degradation; proteome analysis; proteolysis; two dimensional gel electrophoresis; protein identification; matrix assisted laser desorption-ionization
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Eighteen proteins and peptides that were found to change post mortem in Longissimus dorsi from pig muscle were identified by the use of matrix assisted laser desorption/ionization time of flight mass spectrometry. The 18 peptides originate from 9 different proteins including the 3 structural proteins (actin myosin heavy chain and troponin T) and the 6 metabolic proteins glycogen phosphorylase creatine kinase phosphopyruvate hydratase myokinase pyruvate kinase and dihydrolipoamide succinyltransferase. The molecular weight and estimated sequence length of the identified spots show that these fragments result from proteolytic activity in meat. Identification of the parent proteins and the enhanced post mortem appearance of the degradation products make these specific peptides good candidates for meat quality markers and further studies of these specific fragments will lead to a better understanding of the proteolytic activities involved in the post mortem conversion of muscle to meat.
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