By Michael Williams (auth.), Michael Williams (eds.)

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1980) suggested that there was a low degree of bulk tolerance at the 2-position of the purine nucleus. , 1990) being among the most potent A z selective agonists reported. For antagonists, most of which are xanthine in structure, 8phenyl substitution decreases phosphodiesterase inhibitory activity and increases adenosine receptor antagonism (Daly, 1985). Whereas substitution at the 9 position completely eliminates receptor affinity, 1,3, and 7 substitutions can further improve or modify activity with respectto adenosine receptor interactions (Jacobson, 1988).

1980; Schiltz and Brugger, 1982). 1M), high-capacity binding sites (Bmax values =2-30 pmoVmg protein), and inconsistent structure activity data. The ability of tissues to produce large quantities of endogenous adenosine also proved to be a major factor in confusing the data obtained. The more metabolically stable 2-chloroadenosine (2-CADO), although an unstable radioligand, gave better data, with Ktl values in the order of 100 nM (Williams and Risley, unpublished data). It was, however, not until the endogenous adenosine was removed by treatment of the tissue (in this instance, rat brain) with the enzyme (ADA) that high affinity, nanomolar binding of this ligand was observed (Williams and Risley, 1980).

Physiol. Pharmacol. 58,673-691. Bruns, R. F. (1981) Adenosine antagonism by purines, pteridines and benzopteridines in human fibroblasts. Biochem. Pharmacol. 30, 325-333. Bruns, R. F. (1988) Adenosine receptor binding assays, in Adenosine Receptors (Cooper, D. M. F. and Londos, C. ), Liss, New York, pp. 43-62. Bruns, R. , Daly, J. , and Snyder, S. H. (1980) Adenosine receptors in brain membranes: Binding of~-cyclohexylpH]adenosine and 1,3-diethyl-8-PH] phenylxanthine. Proc. Natl. Acad. Sci. USA 77, 5547-5551.

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