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Discrimination between Alkali Metal Cations by Yeast : II. Cation interactions in transport
K(+) is a competitive inhibitor of the uptake of the other alkali metal cations by yeast. Rb(+) is a competitive inhibitor of K(+) uptake, but Li(+), Na(+), and Cs(+) act like H(+). At relatively low concentrations they behave as apparent noncompetitive inhibitors of K(+) transport, but the inhibiti...
Autores principales: | , |
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Formato: | Texto |
Lenguaje: | English |
Publicado: |
The Rockefeller University Press
1967
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2225697/ https://www.ncbi.nlm.nih.gov/pubmed/6034512 |
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author | Armstrong, W. McD. Rothstein, A. |
author_facet | Armstrong, W. McD. Rothstein, A. |
author_sort | Armstrong, W. McD. |
collection | PubMed |
description | K(+) is a competitive inhibitor of the uptake of the other alkali metal cations by yeast. Rb(+) is a competitive inhibitor of K(+) uptake, but Li(+), Na(+), and Cs(+) act like H(+). At relatively low concentrations they behave as apparent noncompetitive inhibitors of K(+) transport, but the inhibition is incomplete. At higher concentrations they inhibit the remaining K(+) transport competitively. Ca(++) and Mg(++) in relatively low concentrations partially inhibit K(+) transport in an apparently noncompetitive manner although their affinity for the transport site is very low. In each case, in concentrations that produce "noncompetitive" inhibition, very little of the inhibiting cation is transported into the cell. Competitive inhibition is accompanied by appreciable uptake of the inhibiting cation. The apparently noncompetitive effect of other cations is reversed by K(+) concentrations much higher than those necessary to essentially "saturate" the transport system. A model is proposed which can account for the inhibition kinetics. This model is based on two cation-binding sites for which cations compete, a carrier or transporting site, and a second nontransporting (modifier) site with a different array of affinities for cations. The association of certain cations with the modifier site leads to a reduction in the turnover of the carrier, the degree of reduction depending on the cation bound to the modifier site and on the cation being transported. |
format | Text |
id | pubmed-2225697 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 1967 |
publisher | The Rockefeller University Press |
record_format | MEDLINE/PubMed |
spelling | pubmed-22256972008-04-23 Discrimination between Alkali Metal Cations by Yeast : II. Cation interactions in transport Armstrong, W. McD. Rothstein, A. J Gen Physiol Article K(+) is a competitive inhibitor of the uptake of the other alkali metal cations by yeast. Rb(+) is a competitive inhibitor of K(+) uptake, but Li(+), Na(+), and Cs(+) act like H(+). At relatively low concentrations they behave as apparent noncompetitive inhibitors of K(+) transport, but the inhibition is incomplete. At higher concentrations they inhibit the remaining K(+) transport competitively. Ca(++) and Mg(++) in relatively low concentrations partially inhibit K(+) transport in an apparently noncompetitive manner although their affinity for the transport site is very low. In each case, in concentrations that produce "noncompetitive" inhibition, very little of the inhibiting cation is transported into the cell. Competitive inhibition is accompanied by appreciable uptake of the inhibiting cation. The apparently noncompetitive effect of other cations is reversed by K(+) concentrations much higher than those necessary to essentially "saturate" the transport system. A model is proposed which can account for the inhibition kinetics. This model is based on two cation-binding sites for which cations compete, a carrier or transporting site, and a second nontransporting (modifier) site with a different array of affinities for cations. The association of certain cations with the modifier site leads to a reduction in the turnover of the carrier, the degree of reduction depending on the cation bound to the modifier site and on the cation being transported. The Rockefeller University Press 1967-03-01 /pmc/articles/PMC2225697/ /pubmed/6034512 Text en Copyright © 1967 by The Rockefeller University Press This article is distributed under the terms of an Attribution–Noncommercial–Share Alike–No Mirror Sites license for the first six months after the publication date (see http://www.rupress.org/terms). After six months it is available under a Creative Commons License (Attribution–Noncommercial–Share Alike 4.0 Unported license, as described at http://creativecommons.org/licenses/by-nc-sa/4.0/). |
spellingShingle | Article Armstrong, W. McD. Rothstein, A. Discrimination between Alkali Metal Cations by Yeast : II. Cation interactions in transport |
title | Discrimination between Alkali Metal Cations by Yeast : II. Cation interactions in transport |
title_full | Discrimination between Alkali Metal Cations by Yeast : II. Cation interactions in transport |
title_fullStr | Discrimination between Alkali Metal Cations by Yeast : II. Cation interactions in transport |
title_full_unstemmed | Discrimination between Alkali Metal Cations by Yeast : II. Cation interactions in transport |
title_short | Discrimination between Alkali Metal Cations by Yeast : II. Cation interactions in transport |
title_sort | discrimination between alkali metal cations by yeast : ii. cation interactions in transport |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2225697/ https://www.ncbi.nlm.nih.gov/pubmed/6034512 |
work_keys_str_mv | AT armstrongwmcd discriminationbetweenalkalimetalcationsbyyeastiicationinteractionsintransport AT rothsteina discriminationbetweenalkalimetalcationsbyyeastiicationinteractionsintransport |