The human intestinal H+/oligopeptide cotransporter hPEPT1 transports differently-charged dipeptides with identical electrogenic properties

被引：49

作者：

Mackenzie, B

Fei, YJ

Ganapathy, V

Leibach, FH

机构：

[1] MED COLL GEORGIA, DEPT BIOCHEM & MOL BIOL, AUGUSTA, GA 30912 USA

[2] UNIV CALIF LOS ANGELES, SCH MED, DEPT PHYSIOL, LOS ANGELES, CA 90095 USA

来源：

BIOCHIMICA ET BIOPHYSICA ACTA-BIOMEMBRANES | 1996年 / 1284卷 / 02期

关键词：

proton-coupled transport; oligopeptide transport; intestinal absorption; membrane transport protein; transporter; Xenopus oocyte;

D O I：

10.1016/S0005-2736(96)00170-8

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

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 1 H+ regardless of the net charge on the driven substrate, and were independent of Na-o(+), K-i(+) and Cl-o(-), calling into the question the familiar concept of the origin of the transporter-mediated current.

引用

页码：125 / 128

页数：4

共 9 条

[1] THE GLIAL-CELL GLUTAMATE UPTAKE CARRIER COUNTERTRANSPORTS PH-CHANGING ANIONS [J].