Abstract
Neuraminidase and slight acid hydrolysis were used to investigate the role of sialic acid residues in the binding of muscarinic agonists and antagonists to membranes from tissues rich in M 1 and M 2 receptors. Membranes were pretreated with neuraminidase at pH 5 and the binding parameters were determined from competitive experiments with ( 3H)-quinuclidinylbenzylate. The removal of sialic acid residues reduced the affinity of muscarinic agonists for cerebellum, heart and lung membranes (M 2), in contrast to striatum (M 1). The affinity of antagonists was not affected. Thus, sialic acid is selectively involved in the interaction of agonists with M 2 muscarinic receptors.
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