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. 1988 Jan 1;249(1):247–253. doi: 10.1042/bj2490247

Distribution and properties of the glycylsarcosine-transport system in rabbit renal proximal tubule. Studies with isolated brush-border-membrane vesicles.

Y Miyamoto 1, J L Coone 1, V Ganapathy 1, F H Leibach 1
PMCID: PMC1148691  PMID: 3342009

Abstract

The distribution and properties of the peptide-transport system in rabbit renal proximal tubule was examined with glycylsarcosine as the substrate and using brush-border-membrane vesicles derived from pars convoluta (outer cortex) and pars recta (outer medulla). The dipeptide was transported into these vesicles against a concentration gradient in the presence of an inward-directed H+ gradient, demonstrating the presence of a H+-coupled peptide-transport system in outer-cortical as well as outer-medullary brush-border membranes. Even though the transport was electrogenic and was energized by a H+ gradient in both membranes, the system was more active in outer medullary membranes than in outer cortical membranes. Kinetic analysis showed that, although the affinity of the transport system for glycylsarcosine was similar in both membrane preparations, the capacity of the system was significantly greater in outer medulla than in outer cortex. In addition, the pH profiles of the peptide-transport systems in these membrane preparations also showed dissimilarities. The greater dipeptide uptake in one membrane vis-à-vis the other may probably be due to the difference in the affinity of the transport system for H+ and/or the difference in peptide/H+ stoichiometry.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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