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Photo affinity labeling of nucleoside transport proteins in plasma membranes isolated from rat and guinea pig liver


, : Photo affinity labeling of nucleoside transport proteins in plasma membranes isolated from rat and guinea pig liver. Biochemical Journal 220(2): 499-506

Nitrobenzylthioinosine (NBMPR) was employed as a probe of the nucleoside transporters from rat and guinea-pig liver. Purified liver plasma membranes prepared on self-generating Percoll density gradients exhibited 16-fold (rat) and 10-fold (guinea pig) higher [3H]NBMPR-binding activities than in crude liver homogenates (3.69 and 14.7 pmol/mg of protein for rat and guinea-pig liver membranes, respectively, and 0.23 and 1.47 pmol/mg of protein for crude liver homogenates, respectively). Binding to membranes from both species was saturable (apparent Kd 0.14 and 0.63 nM for rat and guinea pig membranes, respectively) and inhibited by uridine, adenosine, nitrobenzylthioguanosine (NBTGR) and dilazep. Uridine was an apparent competitive inhibitor of high-affinity NBMPR binding to rat membranes (apparent Ki 1.5 mM). There was a marked species difference with respect to dipyridamole inhibition of NBMPR binding (50% inhibition at 0.2 and > 100 .mu.M for guinea pig and rat, respectively). These results are consistent with a role of NBMPR-binding proteins in liver nucleoside transport. Exposure of rat and guinea pig membranes to high-intensity UV light in the presence of [3H]NBMPR resulted in the selective radiolabeling of membrane proteins which migrated on sodium dodecyl sulfate/polyacrylamide gels with apparent MW values in the same range as that of the human erythrocyte nucleoside transporter (45,000-66,000). Covalent labeling of these proteins was abolished when photolysis was performed in the presence of non-radioactive NBTGR as competing ligand.

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PMID: 6743283


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