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A model for ionic conduction in the ryanodine receptor channel of sheep cardiac muscle sarcoplasmic reticulum
A model is developed for ionic conduction in the sheep cardiac sarcoplasmic reticulum ryanodine receptor channel based on Eyring rate theory. A simple scheme is proposed founded on single-ion occupancy and an energy profile with four barriers and three binding sites. The model is able to quantitativ...
Formato: | Texto |
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Lenguaje: | English |
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The Rockefeller University Press
1992
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2229086/ https://www.ncbi.nlm.nih.gov/pubmed/1279096 |
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collection | PubMed |
description | A model is developed for ionic conduction in the sheep cardiac sarcoplasmic reticulum ryanodine receptor channel based on Eyring rate theory. A simple scheme is proposed founded on single-ion occupancy and an energy profile with four barriers and three binding sites. The model is able to quantitatively predict a large number of conduction properties of the purified and native receptor with monovalent and divalent cations as permeant species. It suggests that discrimination between divalent and monovalent cations is due to a high affinity central binding site and a process that favors the passage of divalent cations between binding sites. Furthermore, differences in conductance among the group Ia cations and among the alkaline earths are largely explained by differing affinity at this putative central binding site. |
format | Text |
id | pubmed-2229086 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 1992 |
publisher | The Rockefeller University Press |
record_format | MEDLINE/PubMed |
spelling | pubmed-22290862008-04-23 A model for ionic conduction in the ryanodine receptor channel of sheep cardiac muscle sarcoplasmic reticulum J Gen Physiol Articles A model is developed for ionic conduction in the sheep cardiac sarcoplasmic reticulum ryanodine receptor channel based on Eyring rate theory. A simple scheme is proposed founded on single-ion occupancy and an energy profile with four barriers and three binding sites. The model is able to quantitatively predict a large number of conduction properties of the purified and native receptor with monovalent and divalent cations as permeant species. It suggests that discrimination between divalent and monovalent cations is due to a high affinity central binding site and a process that favors the passage of divalent cations between binding sites. Furthermore, differences in conductance among the group Ia cations and among the alkaline earths are largely explained by differing affinity at this putative central binding site. The Rockefeller University Press 1992-09-01 /pmc/articles/PMC2229086/ /pubmed/1279096 Text en 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 | Articles A model for ionic conduction in the ryanodine receptor channel of sheep cardiac muscle sarcoplasmic reticulum |
title | A model for ionic conduction in the ryanodine receptor channel of sheep cardiac muscle sarcoplasmic reticulum |
title_full | A model for ionic conduction in the ryanodine receptor channel of sheep cardiac muscle sarcoplasmic reticulum |
title_fullStr | A model for ionic conduction in the ryanodine receptor channel of sheep cardiac muscle sarcoplasmic reticulum |
title_full_unstemmed | A model for ionic conduction in the ryanodine receptor channel of sheep cardiac muscle sarcoplasmic reticulum |
title_short | A model for ionic conduction in the ryanodine receptor channel of sheep cardiac muscle sarcoplasmic reticulum |
title_sort | model for ionic conduction in the ryanodine receptor channel of sheep cardiac muscle sarcoplasmic reticulum |
topic | Articles |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2229086/ https://www.ncbi.nlm.nih.gov/pubmed/1279096 |