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Hepatic transport system of benzylpenicillin was characterized by using freshly prepared rat hepatocytes. Uptake of benzylpenicillin and cefpiramide did not require the presence of sodium ion in the incubation medium. No influence of several kinds of amino acids (leucine, histidine, phenylalanine, valine, alanine, glutamic acid and glycine) and peptides (prolyl-leucine, glycyl-glycine, glycyl-sarcosine, glycyl-leucine and gamma-glutamyl-cysteinylglycine) was observed for benzylpenicillin uptake into hepatocytes. Taurocholic acid and cholic acid significantly inhibited benzylpenicillin uptake. The kinetic study revealed that taurocholic acid inhibited benzylpenicillin uptake in a noncompetitive fashion. A similar effect of benzylpenicillin on taurocholic acid uptake was observed, suggesting that the affinity site of the hepatic transport carrier of benzylpenicillin is distinct from that of taurocholic acid. It is noteworthy that p-aminohippuric acid and p-acetylaminohippuric acid did not inhibit benzylpenicillin uptake. In contrast to the mutual inhibition behavior of benzylpenicillin and taurocholic acid, benzylpenicillin is fully and competitively inhibited by the simultaneous addition of probenecid. The inhibition constant Ki value of probenecid was calculated to be 0.322 mM. The uptake of probenecid was also significantly inhibited by benzylpenicillin. It is postulated that the affinity site of benzylpenicillin transport carrier is the same as that of probenecid and that the whole process of the benzylpenicillin transport system is common, at least in part, to the probenecid transport process in the liver.

journal of pharmacobio-dynamics

Kinetic evidence for a common transport route of benzylpenicillin and probenecid by freshly prepared hepatocytes in rats. Influence of sodium ion, organic anions, amino acids and peptides on benzylpenicillin uptake.