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Subunit selectivity and epitope characterization of mAbs directed against the GABAA/benzodiazepine receptor
mAbs bd 17, bd 24, and bd 28 raised against bovine cerebral gamma- aminobutyric acid (GABAA)/benzodiazepine receptors were analyzed for their ability to detect each of 12 GABAA receptor subunits expressed in cultured mammalian cells. Results showed that mAb bd 17 recognizes epitopes on both beta 2 a...
Formato: | Texto |
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Lenguaje: | English |
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The Rockefeller University Press
1990
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Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2116146/ https://www.ncbi.nlm.nih.gov/pubmed/1693621 |
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collection | PubMed |
description | mAbs bd 17, bd 24, and bd 28 raised against bovine cerebral gamma- aminobutyric acid (GABAA)/benzodiazepine receptors were analyzed for their ability to detect each of 12 GABAA receptor subunits expressed in cultured mammalian cells. Results showed that mAb bd 17 recognizes epitopes on both beta 2 and beta 3 subunits while mAb bd 24 is selective for the alpha 1 subunit of human and bovine, but not of rat origin. The latter antibody reacts with the rat alpha 1 subunit carrying an engineered Leu at position four, documenting the first epitope mapping of a GABAA receptor subunit-specific mAb. In contrast to mAbs bd 17 and bd 24, mAb bd 28 reacts with all GABAA receptor subunits tested but not with a glycine receptor subunit, suggesting the presence of shared epitopes on subunits of GABA-gated chloride channels. |
format | Text |
id | pubmed-2116146 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 1990 |
publisher | The Rockefeller University Press |
record_format | MEDLINE/PubMed |
spelling | pubmed-21161462008-05-01 Subunit selectivity and epitope characterization of mAbs directed against the GABAA/benzodiazepine receptor J Cell Biol Articles mAbs bd 17, bd 24, and bd 28 raised against bovine cerebral gamma- aminobutyric acid (GABAA)/benzodiazepine receptors were analyzed for their ability to detect each of 12 GABAA receptor subunits expressed in cultured mammalian cells. Results showed that mAb bd 17 recognizes epitopes on both beta 2 and beta 3 subunits while mAb bd 24 is selective for the alpha 1 subunit of human and bovine, but not of rat origin. The latter antibody reacts with the rat alpha 1 subunit carrying an engineered Leu at position four, documenting the first epitope mapping of a GABAA receptor subunit-specific mAb. In contrast to mAbs bd 17 and bd 24, mAb bd 28 reacts with all GABAA receptor subunits tested but not with a glycine receptor subunit, suggesting the presence of shared epitopes on subunits of GABA-gated chloride channels. The Rockefeller University Press 1990-06-01 /pmc/articles/PMC2116146/ /pubmed/1693621 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 Subunit selectivity and epitope characterization of mAbs directed against the GABAA/benzodiazepine receptor |
title | Subunit selectivity and epitope characterization of mAbs directed against the GABAA/benzodiazepine receptor |
title_full | Subunit selectivity and epitope characterization of mAbs directed against the GABAA/benzodiazepine receptor |
title_fullStr | Subunit selectivity and epitope characterization of mAbs directed against the GABAA/benzodiazepine receptor |
title_full_unstemmed | Subunit selectivity and epitope characterization of mAbs directed against the GABAA/benzodiazepine receptor |
title_short | Subunit selectivity and epitope characterization of mAbs directed against the GABAA/benzodiazepine receptor |
title_sort | subunit selectivity and epitope characterization of mabs directed against the gabaa/benzodiazepine receptor |
topic | Articles |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2116146/ https://www.ncbi.nlm.nih.gov/pubmed/1693621 |