Veterinary Biosciences - Research Publications

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AMP is a more potent activator of phosphofructokinase-1 activity than fructose 2,6-bisphospate in porcine skeletal muscle under simulated postmortem conditions

Chauhan, SS ; LeMaster, M ; England, EM ; Troy, D ; Ciara, M ; Laura, H ; Kerry, J (Wageningen Academic Publishers, 2017)

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.