The effects of carnosine and anserine on glycolytic reactions in skeletal muscle

Contrary to the reported evidence of Severin and his collaborators, carnosine and anserine were found not to activate the reactions of glycolysis from the break-down of FDP to the formation of PGA. It has been demonstrated that the reported activation could have been due to either an increase in the pH and buffering capacity of the reaction mixture, or to a removal of possible heavy-metal inhibitors as chelated complexes on addition of the dipeptides to the reaction mixture. Although added carnosine phosphate is hydrolyzed in aqueous muscle extracts and has been suggested as the possible ultimate source of muscular contraction energy, neither carnosine phosphate nor anserine phosphate could be identified in muscles containing a high concentration of the free bases.