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The, so far unsuccessful, search for selective effective inhibitors of glycogen phosphorylase for the treatment of type II diabetes has made phosphorylase an active target of research for the last twenty years. Many crystallographic structures of phosphorylase are currently available to aid in this research. However, those structures have been interpreted, at least in part, based on work done with a proteolytically derived form of phosphorylase that lacked the N-terminus (phosphorylase
b’
). It has been reported that phosphorylase
b’
shows no allostery, neither homotropic nor heterotropic. The original report on phosphorylase
b’
examined the allosteric characteristics over very narrow ranges of effector and substrate concentrations, and reported the presence of proteolytic cleavages in addition to the removal of the N-terminus. We have applied molecular biological techniques to generate a truncate lacking the N-terminus with know primary structure, and we have established conditions to fully quantify the allosteric effect of AMP on glycogen phosphorylase
b
. We report here for the first time the full thermodynamic effect of AMP on phosphorylase
b
. Our findings with a truncate lacking the N-terminus show that the effect of AMP binding does not depend on the N-terminus.