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Hormonally regulated phosphoprotein of turkey erythrocytes: localization to plasma membrane
The catecholamine-stimulated cotransport of sodium and potassium ions across the plasma membrane of the turkey erythrocyte was previously found to be associated with increased 32P incorporation into a high molecular weight protein. To determine the subcellular localization of this phosphorylated pro...
Formato: | Texto |
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Lenguaje: | English |
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The Rockefeller University Press
1979
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Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2110436/ https://www.ncbi.nlm.nih.gov/pubmed/229109 |
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collection | PubMed |
description | The catecholamine-stimulated cotransport of sodium and potassium ions across the plasma membrane of the turkey erythrocyte was previously found to be associated with increased 32P incorporation into a high molecular weight protein. To determine the subcellular localization of this phosphorylated protein, which we have termed goblin, a new method has been developed for isolation of pure plasma membranes from turkey erythrocytes. With this method, it has been demonstrated that goblin is located in the plasma membrane. Goblin is not extracted by solutions of low or high ionic strength but is partially extracted by nonionic detergents, indicating that it is not a component of turkey erythrocyte spectrin and suggesting that it may be an intrinsic protein of the plasma membrane. The data are compatible with a possible role for goblin in the hormonal control of ion movements across the plasma membrane. |
format | Text |
id | pubmed-2110436 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 1979 |
publisher | The Rockefeller University Press |
record_format | MEDLINE/PubMed |
spelling | pubmed-21104362008-05-01 Hormonally regulated phosphoprotein of turkey erythrocytes: localization to plasma membrane J Cell Biol Articles The catecholamine-stimulated cotransport of sodium and potassium ions across the plasma membrane of the turkey erythrocyte was previously found to be associated with increased 32P incorporation into a high molecular weight protein. To determine the subcellular localization of this phosphorylated protein, which we have termed goblin, a new method has been developed for isolation of pure plasma membranes from turkey erythrocytes. With this method, it has been demonstrated that goblin is located in the plasma membrane. Goblin is not extracted by solutions of low or high ionic strength but is partially extracted by nonionic detergents, indicating that it is not a component of turkey erythrocyte spectrin and suggesting that it may be an intrinsic protein of the plasma membrane. The data are compatible with a possible role for goblin in the hormonal control of ion movements across the plasma membrane. The Rockefeller University Press 1979-10-01 /pmc/articles/PMC2110436/ /pubmed/229109 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 Hormonally regulated phosphoprotein of turkey erythrocytes: localization to plasma membrane |
title | Hormonally regulated phosphoprotein of turkey erythrocytes: localization to plasma membrane |
title_full | Hormonally regulated phosphoprotein of turkey erythrocytes: localization to plasma membrane |
title_fullStr | Hormonally regulated phosphoprotein of turkey erythrocytes: localization to plasma membrane |
title_full_unstemmed | Hormonally regulated phosphoprotein of turkey erythrocytes: localization to plasma membrane |
title_short | Hormonally regulated phosphoprotein of turkey erythrocytes: localization to plasma membrane |
title_sort | hormonally regulated phosphoprotein of turkey erythrocytes: localization to plasma membrane |
topic | Articles |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2110436/ https://www.ncbi.nlm.nih.gov/pubmed/229109 |