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Distribution of bicarbonate-stimulated ATPase in rat intestinal epithelium
This study reports on the distribution of bicarbonate-stimulated ATPase in rat intestinal epithelial cells. Brush-border membranes and basolateral membranes were separated from each other and from mitochondrial and other intracellular membranes by differential and density gradient centrifugation. Bi...
Formato: | Texto |
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Lenguaje: | English |
Publicado: |
The Rockefeller University Press
1977
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2109899/ https://www.ncbi.nlm.nih.gov/pubmed/140175 |
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collection | PubMed |
description | This study reports on the distribution of bicarbonate-stimulated ATPase in rat intestinal epithelial cells. Brush-border membranes and basolateral membranes were separated from each other and from mitochondrial and other intracellular membranes by differential and density gradient centrifugation. Bicarbonate-sensitive ATPase activity followed the mitochondrial marker succinic dehydrogenase closely throughout all the centrifugation steps. The low HCO3--ATPase activity in purified brush-border and basolateral plasma membranes could be accounted for quantitatively by the small mitochondrial contamination. Consequently, there are no grounds for postulating that this enzyme has a direct role in H+ or HCO3- transport across the rat small intestine. |
format | Text |
id | pubmed-2109899 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 1977 |
publisher | The Rockefeller University Press |
record_format | MEDLINE/PubMed |
spelling | pubmed-21098992008-05-01 Distribution of bicarbonate-stimulated ATPase in rat intestinal epithelium J Cell Biol Articles This study reports on the distribution of bicarbonate-stimulated ATPase in rat intestinal epithelial cells. Brush-border membranes and basolateral membranes were separated from each other and from mitochondrial and other intracellular membranes by differential and density gradient centrifugation. Bicarbonate-sensitive ATPase activity followed the mitochondrial marker succinic dehydrogenase closely throughout all the centrifugation steps. The low HCO3--ATPase activity in purified brush-border and basolateral plasma membranes could be accounted for quantitatively by the small mitochondrial contamination. Consequently, there are no grounds for postulating that this enzyme has a direct role in H+ or HCO3- transport across the rat small intestine. The Rockefeller University Press 1977-04-01 /pmc/articles/PMC2109899/ /pubmed/140175 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 Distribution of bicarbonate-stimulated ATPase in rat intestinal epithelium |
title | Distribution of bicarbonate-stimulated ATPase in rat intestinal epithelium |
title_full | Distribution of bicarbonate-stimulated ATPase in rat intestinal epithelium |
title_fullStr | Distribution of bicarbonate-stimulated ATPase in rat intestinal epithelium |
title_full_unstemmed | Distribution of bicarbonate-stimulated ATPase in rat intestinal epithelium |
title_short | Distribution of bicarbonate-stimulated ATPase in rat intestinal epithelium |
title_sort | distribution of bicarbonate-stimulated atpase in rat intestinal epithelium |
topic | Articles |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2109899/ https://www.ncbi.nlm.nih.gov/pubmed/140175 |