Binding of amino beta-lactam antibiotics to soluble protein from rat intestinal mucosa--II. Mutual inhibition of binding among amino beta-lactam antibiotics and binding characteristics.

  title={Binding of amino beta-lactam antibiotics to soluble protein from rat intestinal mucosa--II. Mutual inhibition of binding among amino beta-lactam antibiotics and binding characteristics.},
  author={Ken Iseki and K Mori and K Miyazaki and T. Arita},
  journal={Biochemical pharmacology},
  volume={36 11},
The characteristics of binding of amino beta-lactam antibiotics including ampicillin, amoxicillin, cephalexin and cephradine to fraction b obtained from the 105,000 g supernatant of rat small intestinal mucosa was investigated. The mutual inhibition of binding among these antibiotics was observed, and these were dependent on the concentration of inhibitors. It was found that dipeptides such as L-carnosine and glycylglycine significantly reduced the binding of cephalexin to fraction b, but the… 
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Comparison of Transport Characteristics of Amino β‐Lactam Antibiotics and Dipeptides Across Rat Intestinal Brush Border Membrane
The results suggest that the contribution of the inward H+ gradient to the permeation of ampicillin, cephradine and glycylglycine across the rat small intestinal brush border membranes is different for each of the substances examined.
Intestinal Absorption Mechanisms of β-Lactam Antibiotics
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Effect of Chlorpromazine on the Permeability of β‐Lactam Antibiotics Across Rat Intestinal Brush Border Membrane Vesicles
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The intestinal peptide carrier: A potential transport system for small peptide derived drugs
Abstract Several laboratories have recently shown that many peptides and peptide-type drugs are absorbed in the small intestine via the peptide transporter for nutrient di-and tripeptides. The
Contribution of Passive Transport Mechanisms to the Intestinal Absorption of β‐Lactam Antibiotics
Results suggest that the β‐lactam antibiotics tested, like L‐glucose, pass through the rat intestinal brush border membrane mainly by passive diffusion, however, the differences in absorption between these drugs cannot be explained by a simple permeation process alone.


Intestinal absorption of several beta-lactam antibiotics. V. Effect of amino beta-lactam analogues and dipeptides on the absorption of amino beta-lactam antibiotics.
The result suggest that the carrier-mediated transport system correlated to dipeptides participates only to a small degree in the common absorption mechanisms of these amino beta-lactam antibiotics.
Mutual effects of amino-beta-lactam antibiotics and glycylglycine on the transmural potential difference in the small intestinal epithelium of rats.
The results suggest that amino-beta-lactam antibiotic-induced PDt relates to the Na+ ion fluxes as reported for dipeptides.
Kinetics and mechanism of in vitro uptake of amino-beta-lactam antibiotics by rat small intestine and relation to the intact-peptide transport system.
This is the first report which establishes, from a kinetic point of view, the involvement of a common transport system in the in vitro uptakes of the dipeptides and the antibiotics.
Intestinal absorption of several beta-lactam antibiotics. III. Competitive inhibition behavior among zwitterionic beta-lactam antibiotics in the rat intestinal absorption.
Results showed that cephradine had a common carrier-mediated transport mechanism with cyclacillin which is not present in the absorption process of cephalexin, which was postulated to be based on the competitive inhibition in the accumulation or uptake by the intestinal mucosa.
Intestinal absorption of several beta-lactam antibiotics. II. Absorption characteristics of amino-penicillins and amino-cephalosporins.
The accumulations of these drugs, especially cephalexin and cephradine, were particularly marked, and the accumulation of each of these three drugs was significantly inhibited at low temperature, providing an experimental basis for the known rapid absorption of these antibiotics.
Binding protein for 1-anilino-8-naphthalenesulfonate in rat liver cytoplasm.
The Z-fraction in rat liver cytoplasm was found to contain three protein fractions having fairly high binding activities for ANS and sulfobromophthalein (BSP), and the D 2 -fraction, which eluted earlier on a DEAE-Sephadex column, had the highest binding affinity for these anions.
Comparison of binding of thyroid hormone analogues to hepatic organic anion binding proteins.
The binding affinities of these organic anions binders are 2-3 orders of magnitude lower than an hepatic cytosolic thyroid binder reported by others, suggesting that ligandin and organic anion binder may not be important in intracellular thyroid hormone transfer.
Fluorescence of 1,8-anilinonaphthalene sulfonic acid bound to proteins and to lipids of sarcolemma.
Results of analyses of spectra obtained with various concentrations of sarcolemma and 1,8-anilinonaphthalene sulfonic acid suggest that the proteins have a higher affinity, but only about half the binding capacity for 1, 8-anILinonphthalene sulphonic acid as do lipids.
Interaction of a fluorescent probe with erythrocyte membrane and lipids: Effects of local anesthetics and calcium
Changes in ANS fluorescence observed in mitochondria during active calcium transport, or upon the addition of substrate and oxygen, have been interpreted as demonstrating conformational changes in the membranes.
Protein measurement with the Folin phenol reagent.
Procedures are described for measuring protein in solution or after precipitation with acids or other agents, and for the determination of as little as 0.2 gamma of protein.