Transport of Charged Dipeptides by the Intestinal H+/Peptide Symporter PepT1 Expressed in Xenopus laevis Oocytes

@article{Amasheh1997TransportOC,
  title={Transport of Charged Dipeptides by the Intestinal H+/Peptide Symporter PepT1 Expressed in Xenopus laevis Oocytes},
  author={Salah Amasheh and U Wenzel and Michael Boll and David Dorn and W. -M. Weber and Wolfgang Clauss and Hannelore Daniel},
  journal={The Journal of Membrane Biology},
  year={1997},
  volume={155},
  pages={247-256}
}
The cloned intestinal peptide transporter is capable of electrogenic H+-coupled cotransport of neutral di- and tripeptides and selected peptide mimetics. Since the mechanism by which PepT1 transports substrates that carry a net negative or positive charge at neutral pH is poorly understood, we determined in Xenopus oocytes expressing PepT1 the characteristics of transport of differently charged glycylpeptides. Transport function of PepT1 was assessed by flux studies employing a radiolabeled… CONTINUE READING

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