2-Chloro-[3H]-adenosine binding in isolated rat kidney membranes.

Binding sites for 2-chloro-[3H]-adenosine were found to be present in rat kidney membranes. Binding was inhibited by adenosine receptor agonists (5'-N-ethylcarboxamide adenosine, NECA; L-phenylisopropyl adenosine, L-PIA) and antagonists (theophylline; 3-isobutyl-1-methylxanthine, IBMX) but unaffected by an adenosine uptake inhibitor (papaverine). The binding sites exhibited the properties of an adenosine A2 receptor: micromolar affinity for 2-chloroadenosine; nearly identical potencies of theophylline and IBMX for inhibition of binding; NECA more potent than L-PIA for inhibition of binding.