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pubmed-article:1676599pubmed:abstractTextThe existence of an endogenous Na(+)-glutamate cotransporter in the oocytes of Xenopus laevis is demonstrated. The transporter does not accept D-glutamate as substrate. The dependence on substrate displays two saturating components with low (K1/2 = 9 mM) and high (K1/2 = 0.35 microM) affinities for L-glutamate. The dependence on external Na+ exhibits a saturating component with a K1/2 value of about 5 mM and a component that has not saturated up to 110 mM Na+. In voltage-clamped oocytes, it is possible to demonstrate that Na(+)-dependent L-glutamate transport is directly coupled to countertransport of Rb+. The analysis of the voltage dependence of the Na+,K(+)-dependent L-glutamate uptake suggests that positive charges are moved inwardly during the transport cycle.lld:pubmed
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pubmed-article:1676599pubmed:dateRevised2006-11-15lld:pubmed
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pubmed-article:1676599pubmed:articleTitleEndogenous L-glutamate transport in oocytes of Xenopus laevis.lld:pubmed
pubmed-article:1676599pubmed:affiliationMax-Planck-Institut für Biophysik, Frankfurt/Main, F.R.G.lld:pubmed
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