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  Peptide transport in rabbit intestinal brush-border membrane vesicles studied with a potential-sensitive dye

Ganapathy, V., Burckhardt, G., & Leibach, F. H. (1985). Peptide transport in rabbit intestinal brush-border membrane vesicles studied with a potential-sensitive dye. Biochimica et Biophysica Acta-Biomembranes, 816(2), 234-240. doi:10.1016/0005-2736(85)90490-0.

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 Creators:
Ganapathy, Vadivel1, Author
Burckhardt, Gerhard2, Author           
Leibach, Frederick H.1, Author
Affiliations:
1Department of Cell and Molecular Biology, Medical College of Georgia, Augusta, GA 30912 U.S.A., ou_persistent22              
2Department of Physiology, Max Planck Institute of Biophysics, Max Planck Society, ou_2068297              

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Free keywords: Peptide transport; Na+ independence; Electrogenic transport; Potential-sensitive dye; Brush-border membrane; (Rabbit intestine)
 Abstract: Peptide transport in purified rabbit intestinal brush-border membrane vesicles has been studied using a potential-sensitive fluorescent dye, di-S-C3(5). Transport of dipeptides is accompanied by an increase in the fluorescence of the dye in the presence and absence of Na+, indicating electrogenic, Na+-independent peptide transport. Dipeptides containing d-amino acids also increase the fluorescence, showing that these peptides too possess significant affinity for the peptide transport system. β-Alanylglycylglycine and prolylglycylglycine, very much like the dipeptides, increase the fluorescence even in the absence of Na+ which demonstrates the Na+-independent, electrogenic transport of tripeptides. However, concentrations needed for half-maximal fluorescence changes are higher for tripeptides than for dipeptides suggesting different affinities for the carriers. The studies, in addition, provide evidence for the existence of more than one carrier system for translocation of small peptides in rabbit intestinal brush-border membrane.

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Language(s): eng - English
 Dates: 1985-01-292002-12-191985-06-27
 Publication Status: Issued
 Pages: 7
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Identifiers: DOI: 10.1016/0005-2736(85)90490-0
PMID: 3839134
 Degree: -

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Title: Biochimica et Biophysica Acta-Biomembranes
Source Genre: Journal
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Publ. Info: Amsterdam : Elsevier
Pages: - Volume / Issue: 816 (2) Sequence Number: - Start / End Page: 234 - 240 Identifier: ISSN: 0005-2736
CoNE: https://pure.mpg.de/cone/journals/resource/954926938702