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  • Title: Characterization of p-aminohippurate transport from rat kidney which is expressed after injection of size-selected mRNA into oocytes of Xenopus laevis.
    Author: Steffgen J, Scheyerl F, Gründemann D, Kienle S, Franz HE, Koepsell H.
    Journal: Biochim Biophys Acta; 1993 Jun 18; 1149(1):145-50. PubMed ID: 8318526.
    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.
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