AJP - GI Watch the video to see how APS reaches out to developing nations.
HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
 QUICK SEARCH:   [advanced]


     


Am J Physiol Gastrointest Liver Physiol 248: G682-G686, 1985;
0193-1857/85 $5.00
This Article
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Citing Articles
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Rajendran, V. M.
Right arrow Articles by Ramaswamy, K.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Rajendran, V. M.
Right arrow Articles by Ramaswamy, K.

AJP - Gastrointestinal and Liver Physiology, Vol 248, Issue 6 682-G686, Copyright © 1985 by American Physiological Society


ARTICLES

Transport of glycyl-L-proline by mouse intestinal brush-border membrane vesicles

V. M. Rajendran, A. Berteloot and K. Ramaswamy

The characteristics of [14C]glycyl-L-proline transport have been studied using brush-border membrane vesicles from mouse small intestine in order to investigate the transport of nonhydrolyzable peptide across the brush-border membrane. Uptake curves for the peptide did not exhibit overshoot phenomena and were similar under Na+ or K+ gradient conditions (extravesicular greater than intravesicular). However, L-proline was transported by Na+ gradient-dependent system. Analysis of the incubation medium and the intravesicular contents showed that there was negligible hydrolysis of the peptide. Transport of glycyl-L-proline was saturable, conforming to Michaelis-Menten kinetics with a Km of 30.8 +/- 1.9 mM and a Vmax of 5.96 +/- 0.17 nmol.mg prot-1.0.4 min-1. Uptake of glycyl-L-proline was not significantly inhibited by free amino acids nor by most of the peptides containing D amino acids but was strongly inhibited (up to 64%) by various di- and tripeptides of L amino acids. These results clearly show that glycyl-L-proline was transported by a Na+-independent, carrier-mediated process. Our results suggest that the nonhydrolyzable peptides are transported mostly by carrier-mediated processes in contrast to hydrolyzable peptides.





HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
Visit Other APS Journals Online