Nitrobenzylthionionosine binding sites in the erythrocyte membrane.
Nitrobenzylthioinosine binds tightly, but reversibly, to sites in the human erythrocyte membrane; occupancy of these sites blocks the transport of uridine and of other nucleosides. This report described the inhibition of nitrobenzylthioinosine binding at these sites by substrates of the uridine transport mechanism and by compounds related to nitrobenzylthioinosine. For some of these compounds dissociation constants for binding at the nitrobenzylthioinosine sites were determined, assumming competition with nitrobenzylthioinosine. Deoxycytidine, a substrate for the uridine transport mechanism, did not inhibit binding of nitrobenzylthioinosine, suggesting that binding sites for the latter are distinct from nucleoside sites directly involved in transport.
D001665:Binding Sites; D001667:Binding, Competitive; D001693:Biological Transport, Active; D002462:Cell Membrane / Q000187:drug effects / Q000378:metabolism*; D004912:Erythrocytes / Q000187:drug effects / Q000378:metabolism*; D006801:Humans; D007288:Inosine / Q000031:analogs & derivatives* / Q000494:pharmacology; D007700:Kinetics; D009578:Nitrobenzenes / Q000097:blood / Q000494:pharmacology; D011402:Pronase / Q000494:pharmacology; D011485:Protein Binding; D013868:Thioinosine / Q000031:analogs & derivatives* / Q000097:blood; D014357:Trypsin / Q000494:pharmacology; D014529:Uridine / Q000378:metabolism
D009578:Nitrobenzenes; D013868:Thioinosine; D007288:Inosine; D014357:Trypsin; D011402:Pronase; D014529:Uridine