Solubilization and reconstitution characteristics of the carrier protein(s) responsible for the transport of ceftibuten, a substrate for the oligopeptide transporters, in rat renal brush-border membrane
Author:
Publisher
Elsevier BV
Subject
Cell Biology,Biochemistry,Biophysics
Reference31 articles.
1. The high and low affinity transport systems for dipeptides in kidney brush border membrane respond differently to alterations in pH gradient and membrane potential.
2. Influence of amino acid side-chain modification on the uptake system for β-lactam antibiotics and dipeptides from rabbit small intestine
3. Target size analysis of the peptide/H+-symporter in kidney brush-border membranes
4. Molecular cloning of PEPT 2, a new member of the H+/peptide cotransporter family, from human kidney
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1. Structure and function of eukaryotic peptide transporters;Cellular and Molecular Life Sciences (CMLS);2000-05-01
2. Compartmentalization and transport in beta-lactam antibiotic biosynthesis by filamentous fungi;Antonie van Leeuwenhoek;1999
3. Apical uptake of radiolabelled ochratoxin A into Madin–Darby canine kidney cells;Toxicology;1998-11
4. Structural studies of the H + /oligopeptide transport system from rabbit small intestine;Biochimica et Biophysica Acta (BBA) - Biomembranes;1998-08
5. Purification by ceftibuten-affinity chromatography and the functional reconstitution of oligopeptide transporter(s) in rat intestinal brush-border membrane;Biochimica et Biophysica Acta (BBA) - Biomembranes;1998-03
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