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Histidine Transport in Plasma Membrane Vesicles from Rat Liver

Overview
Journal Pflugers Arch
Specialty Physiology
Date 1988 Mar 1
PMID 3380646
Citations 4
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Abstract

The transport of L-histidine, a selective substrate for system N, across liver plasma membrane vesicles has been studied. The amino acid is accumulated sevenfold within the intravesicular space in the presence of a sodium gradient. Lithium can replace sodium to some extent in the cotransport mechanism. The amino acid translocation is not influenced by the transmembrane electrical potential difference. Histidine kinetics involves a saturable component plus a linear one both in the presence and in the absence of sodium. Sodium affects mainly the affinity of the translocator and to a lesser extent its mobility. Histidine uptake is competitively inhibited by glutamine and it is affected by alanine in a noncompetitive manner.

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