Cass C E, Paterson A R
Biochim Biophys Acta. 1976 Jan 21;419(2):285-94. doi: 10.1016/0005-2736(76)90354-0.
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.
硝基苄硫代肌苷与人红细胞膜上的位点紧密但可逆地结合；这些位点被占据会阻断尿苷及其他核苷的转运。本报告描述了尿苷转运机制的底物以及与硝基苄硫代肌苷相关的化合物对硝基苄硫代肌苷在这些位点结合的抑制作用。对于其中一些化合物，在假设与硝基苄硫代肌苷存在竞争的情况下，测定了它们在硝基苄硫代肌苷位点的结合解离常数。脱氧胞苷是尿苷转运机制的一种底物，它并不抑制硝基苄硫代肌苷的结合，这表明后者的结合位点与直接参与转运的核苷位点不同。
