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Characterization of p-aminohippurate transport from rat kidney which is expressed after injection of size-selected mRNA into oocytes of Xenopus laevis

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Gründemann,  Dirk
Department of Physiology, Max Planck Institute of Biophysics, Max Planck Society;

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Koepsell,  Hermann
Department of Physiology, Max Planck Institute of Biophysics, Max Planck Society;

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Citation

Steffgen, J., Scheyerl, F., Gründemann, D., Kienle, S., Franz, H. E., & Koepsell, H. (1993). Characterization of p-aminohippurate transport from rat kidney which is expressed after injection of size-selected mRNA into oocytes of Xenopus laevis. Biochimica et Biophysica Acta-Biomembranes, 1149(1), 145-150. doi:10.1016/0005-2736(93)90035-x.


Cite as: https://hdl.handle.net/21.11116/0000-0008-28D8-8
Abstract
First, the existence of an endogenous p-aminohippurate (PAH) transporter in oocytes of Xenopus laevis was demonstrated. When, however, the oocytes were injected with mRNA from rat kidney cortex, an expressed p-aminohippuric acid (PAH) uptake was seen which differed from the endogenous transporter. Both transport systems are saturated at high PAH concentrations, exhibit trans-stimulation by PAH and are partially inhibited by probenecid. The endogenous transport has a rather low affinity for PAH (Km = 0.57 mM) and is about 50% inhibited by probenecid (one apparent inhibition site with half maximal inhibition at 0.5 mM). The expressed PAH transport has a high affinity for PAH (Km = 60 microM) and can be inhibited 80% by probenecid (two apparent inhibition sites with half maximal inhibitions at 1 microM and 2 mM). Expression experiments with fractionated mRNA revealed that the PAH transport expressed from rat kidney cortex is encoded by an mRNA of 1.8 to 2.5 kb.