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

Download
Citations
Altmetric
Author
Chauhan, SS; LeMaster, M; England, EMEditor
Troy, D; Ciara, M; Laura, H; Kerry, JDate
2017Source Title
63rd International Congress of Meat Science and TechnologyPublisher
Wageningen Academic PublishersAffiliation
Veterinary and Agricultural SciencesAgriculture and Food Systems
Metadata
Show full item recordDocument Type
Conference PaperCitations
Chauhan, 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 Status
Open AccessAbstract
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.
Export Reference in RIS Format
Endnote
- Click on "Export Reference in RIS Format" and choose "open with... Endnote".
Refworks
- Click on "Export Reference in RIS Format". Login to Refworks, go to References => Import References