Lysine transport by brush-border membrane vesicles of eel intestine: interaction with neutral amino acids.
L-[H-3] lysine uptake was measured in brush-border membrane vesicles prepared from intestinal mucosa of the European eel Anguilla anguilla. Lysine uptake occurred via 1) a nonsaturable component with an apparent diffusional permeability (P) of 0.58-mu-l.mg protein-1.min-1, 2) a Na-dependent transpor...
Main Authors: | , , , , |
---|---|
Other Authors: | , , , , |
Format: | Article in Journal/Newspaper |
Language: | English |
Published: |
1990
|
Subjects: | |
Online Access: | http://hdl.handle.net/11587/105214 |
id |
ftunivsalento:oai:iris.unisalento.it:11587/105214 |
---|---|
record_format |
openpolar |
spelling |
ftunivsalento:oai:iris.unisalento.it:11587/105214 2024-04-21T07:45:32+00:00 Lysine transport by brush-border membrane vesicles of eel intestine: interaction with neutral amino acids. VILELLA, Sebastiano MAFFIA, Michele STORELLI, Carlo G. A. AHEARN G. CASSANO Vilella, Sebastiano G. A., Ahearn G., Cassano Maffia, Michele Storelli, Carlo 1990 STAMPA http://hdl.handle.net/11587/105214 eng eng info:eu-repo/semantics/altIdentifier/wos/A1990EQ38700059 volume:259 firstpage:R1181 lastpage:R1188 numberofpages:8 journal:AMERICAN JOURNAL OF PHYSIOLOGY http://hdl.handle.net/11587/105214 info:eu-repo/semantics/altIdentifier/scopus/s2.0-0025670385 AMINO ACID TRANSPORT SODIUM-DEPENDENT TRANSPORT SODIUM-INDEPENDENT TRANSPORT COTRANSPORT EPITHELIAL TRANSPORT NUTRIENT ABSORPTION COMPETITIVE INHIBITION ANGUILLA-ANGUILLA info:eu-repo/semantics/article 1990 ftunivsalento 2024-03-28T01:39:35Z L-[H-3] lysine uptake was measured in brush-border membrane vesicles prepared from intestinal mucosa of the European eel Anguilla anguilla. Lysine uptake occurred via 1) a nonsaturable component with an apparent diffusional permeability (P) of 0.58-mu-l.mg protein-1.min-1, 2) a Na-dependent transport system [half-saturation constant (K(app)) 0.16 mM, maximal transport rate (J(max)) 3.57 nmol.mg protein-1.min-1]; 3) a Na-independent transport system (K(app) 0.17 mM, J(max) 2.77 nmol.mg protein-1.min-1). Both carrier-mediated processes were accelerated by the presence of an intravesicular negative membrane potential. Hill analysis of L-lysine influx, over a wide range of external Na concentrations, resulted in a Hill coefficient (n) of approximately 2, suggesting that two or more Na ions may be associated with amino acid transport. The inhibition of lysine uptake by other amino acids was studied. Na-dependent lysine uptake was competitively inhibited by proline [inhibitory constant (K(i)) approximately 2 mM] and may occur by a system specific for cationic amino acids. Na-independent lysine uptake was competitively inhibited by alanine (K(i) approximately 1 mM) and may occur by a classic L system. Article in Journal/Newspaper Anguilla anguilla Università del Salento: CINECA IRIS |
institution |
Open Polar |
collection |
Università del Salento: CINECA IRIS |
op_collection_id |
ftunivsalento |
language |
English |
topic |
AMINO ACID TRANSPORT SODIUM-DEPENDENT TRANSPORT SODIUM-INDEPENDENT TRANSPORT COTRANSPORT EPITHELIAL TRANSPORT NUTRIENT ABSORPTION COMPETITIVE INHIBITION ANGUILLA-ANGUILLA |
spellingShingle |
AMINO ACID TRANSPORT SODIUM-DEPENDENT TRANSPORT SODIUM-INDEPENDENT TRANSPORT COTRANSPORT EPITHELIAL TRANSPORT NUTRIENT ABSORPTION COMPETITIVE INHIBITION ANGUILLA-ANGUILLA VILELLA, Sebastiano MAFFIA, Michele STORELLI, Carlo G. A. AHEARN G. CASSANO Lysine transport by brush-border membrane vesicles of eel intestine: interaction with neutral amino acids. |
topic_facet |
AMINO ACID TRANSPORT SODIUM-DEPENDENT TRANSPORT SODIUM-INDEPENDENT TRANSPORT COTRANSPORT EPITHELIAL TRANSPORT NUTRIENT ABSORPTION COMPETITIVE INHIBITION ANGUILLA-ANGUILLA |
description |
L-[H-3] lysine uptake was measured in brush-border membrane vesicles prepared from intestinal mucosa of the European eel Anguilla anguilla. Lysine uptake occurred via 1) a nonsaturable component with an apparent diffusional permeability (P) of 0.58-mu-l.mg protein-1.min-1, 2) a Na-dependent transport system [half-saturation constant (K(app)) 0.16 mM, maximal transport rate (J(max)) 3.57 nmol.mg protein-1.min-1]; 3) a Na-independent transport system (K(app) 0.17 mM, J(max) 2.77 nmol.mg protein-1.min-1). Both carrier-mediated processes were accelerated by the presence of an intravesicular negative membrane potential. Hill analysis of L-lysine influx, over a wide range of external Na concentrations, resulted in a Hill coefficient (n) of approximately 2, suggesting that two or more Na ions may be associated with amino acid transport. The inhibition of lysine uptake by other amino acids was studied. Na-dependent lysine uptake was competitively inhibited by proline [inhibitory constant (K(i)) approximately 2 mM] and may occur by a system specific for cationic amino acids. Na-independent lysine uptake was competitively inhibited by alanine (K(i) approximately 1 mM) and may occur by a classic L system. |
author2 |
Vilella, Sebastiano G. A., Ahearn G., Cassano Maffia, Michele Storelli, Carlo |
format |
Article in Journal/Newspaper |
author |
VILELLA, Sebastiano MAFFIA, Michele STORELLI, Carlo G. A. AHEARN G. CASSANO |
author_facet |
VILELLA, Sebastiano MAFFIA, Michele STORELLI, Carlo G. A. AHEARN G. CASSANO |
author_sort |
VILELLA, Sebastiano |
title |
Lysine transport by brush-border membrane vesicles of eel intestine: interaction with neutral amino acids. |
title_short |
Lysine transport by brush-border membrane vesicles of eel intestine: interaction with neutral amino acids. |
title_full |
Lysine transport by brush-border membrane vesicles of eel intestine: interaction with neutral amino acids. |
title_fullStr |
Lysine transport by brush-border membrane vesicles of eel intestine: interaction with neutral amino acids. |
title_full_unstemmed |
Lysine transport by brush-border membrane vesicles of eel intestine: interaction with neutral amino acids. |
title_sort |
lysine transport by brush-border membrane vesicles of eel intestine: interaction with neutral amino acids. |
publishDate |
1990 |
url |
http://hdl.handle.net/11587/105214 |
genre |
Anguilla anguilla |
genre_facet |
Anguilla anguilla |
op_relation |
info:eu-repo/semantics/altIdentifier/wos/A1990EQ38700059 volume:259 firstpage:R1181 lastpage:R1188 numberofpages:8 journal:AMERICAN JOURNAL OF PHYSIOLOGY http://hdl.handle.net/11587/105214 info:eu-repo/semantics/altIdentifier/scopus/s2.0-0025670385 |
_version_ |
1796940549145493504 |