Abstract
Carnosine (β-alanyl-L-histidine) activates rabbit muscle phosphorylase a in the presence and absence of AMP and phosphorylase b in the presence of AMP in a biphasic manner with a maximal activation at about 50mM carnosine and with phosphorylase b showing a greater degree of activation than phosphorylase a . Anserine (β-alanyl-L-N π-methyl-histidine) activates phosphorylase a to a lesser extent than carnosine up to a concentration of 90mM, whereas with phosphorylase b a weak activation below 30mM and a concentration-dependent inhibition above this concentration occurs. These effects are specific for the dipeptides and are not shown by their constituent amino acids. Carnosine and anserine activate phosphorylase a in the presence of the allosteric inhibitors ATP, D-glucose and caffeine, and the inhibition of phosphorylase b by anserine is also observed in the presence of these inhibitors.
Published Version
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