Saturable, high affinity binding of the nucleoside transport inhibitor, nitrobenzylthioinosine, to guinea pig cardiac membranes.
The site-specific binding of the potent nucleoside transport inhibitor, [3H]nitrobenzylthioinosine ([3H]NBMPR), to guinea pig cardiac membranes was rapid, reversible and saturable. [3H]NBMPR bound with high affinity to a single class of sites at which the KD was 0.23 +/- 0.07 nM and which had a Bmax of 1700 +/- 290 fmol/mg protein. Several recognized nucleoside transport inhibitors and benzodiazepines inhibited the binding of [3H]NBMPR with an order of potency similar to that observed for the inhibition of the binding of [3H]NBMPR to human erythrocytes and guinea pig synaptosomes.
D000818:Animals; D014151:Anti-Anxiety Agents / Q000494:pharmacology; D001569:Benzodiazepines; D001665:Binding Sites / Q000187:drug effects; D001692:Biological Transport; D004109:Dilazep / Q000494:pharmacology; D004176:Dipyridamole / Q000494:pharmacology; D005260:Female; D006168:Guinea Pigs; D066298:In Vitro Techniques; D007288:Inosine / Q000031:analogs & derivatives*; D008566:Membranes / Q000378:metabolism; D009206:Myocardium / Q000378:metabolism*; D013868:Thioinosine / Q000031:analogs & derivatives* / Q000494:pharmacology
D014151:Anti-Anxiety Agents; D001569:Benzodiazepines; D013868:Thioinosine; D007288:Inosine; D004176:Dipyridamole; D004109:Dilazep; C001789:4-nitrobenzylthioinosine