The human intestinal H+/oligopeptide cotransporter hPEPT1 transports differently-charged dipeptides with identical electrogenic properties
B Mackenzie, YJ Fei, V Ganapathy… - Biochimica et Biophysica …, 1996 - Elsevier
B Mackenzie, YJ Fei, V Ganapathy, FH Leibach
Biochimica et Biophysica Acta (BBA)-Biomembranes, 1996•ElsevierThe human intestinal H+/oligopeptide cotransporter hPEPT1, expressed in Xenopus
oocytes, transported neutral, anionic and cationic dipeptides with identical electrogenic
properties and maximal evoked currents. Currents were activated by I H+ regardless of the
net charge on the driven substrate, and were independent of Nao+, Ki+ and Clo−, calling
into question the familiar concept of the origin of the transporter-mediated current.
oocytes, transported neutral, anionic and cationic dipeptides with identical electrogenic
properties and maximal evoked currents. Currents were activated by I H+ regardless of the
net charge on the driven substrate, and were independent of Nao+, Ki+ and Clo−, calling
into question the familiar concept of the origin of the transporter-mediated current.
The human intestinal H+/oligopeptide cotransporter hPEPT1, expressed in Xenopus oocytes, transported neutral, anionic and cationic dipeptides with identical electrogenic properties and maximal evoked currents. Currents were activated by I H+ regardless of the net charge on the driven substrate, and were independent of Nao+, Ki+ and Clo−, calling into question the familiar concept of the origin of the transporter-mediated current.
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