AMP is a more potent activator of phosphofructokinase-1 activity than fructose 2,6-bisphospate in porcine skeletal muscle under simulated postmortem conditions
AuthorChauhan, SS; LeMaster, M; England, EM
EditorTroy, D; Ciara, M; Laura, H; Kerry, J
Source Title63rd International Congress of Meat Science and Technology
PublisherWageningen Academic Publishers
AffiliationVeterinary and Agricultural Sciences
Agriculture and Food Systems
Document TypeConference Paper
CitationsChauhan, S. S., LeMaster, M. & England, E. M. (2017). AMP is a more potent activator of phosphofructokinase-1 activity than fructose 2,6-bisphospate in porcine skeletal muscle under simulated postmortem conditions. Troy, D (Ed.) Ciara, M (Ed.) Laura, H (Ed.) Kerry, J (Ed.) 63rd International Congress of Meat Science and Technology, Wageningen Academic Publishers.
Access StatusOpen Access
Phosphofructokinase-1 (PFK-1) is a key regulatory enzyme of postmortem glycolysis. PFK-1’s activity is regulated antemortem by a number of compounds including adenosine monophosphate (AMP) and fructose 2,6-bisphosphate (F-2,6-BP). However, PFK-1’s postmortem regulation by AMP and F-2,6-BP is still unclear. Therefore, a study was conducted where porcine longissimus lumborum samples were collected to determine PFK-1 activity as affected by various concentrations of AMP and F-2,6-BP at buffered pH. Both compounds increased PFK-1 activity. However, at physiological concentrations, 50 and 150 μM AMP increased PFK-1 activity compared to 1 and 2 μM F-2,6-BP. Thus, AMP may play a greater role in dictating the rate and extent of postmortem glycolysis and pH decline than F-2,6-BP.
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