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Large-scale purification of presynaptic plasma membranes from Torpedo marmorata electric organ
The presynaptic plasma membrane (PSPM) of cholinergic nerve terminals was purified from Torpedo electric organ using a large-scale procedure. Up to 500 g of frozen electric organ were fractioned in a single run, leading to the isolation of greater than 100 mg of PSPM proteins. The purity of the frac...
Formato: | Texto |
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Lenguaje: | English |
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The Rockefeller University Press
1985
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Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2113949/ https://www.ncbi.nlm.nih.gov/pubmed/2997233 |
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collection | PubMed |
description | The presynaptic plasma membrane (PSPM) of cholinergic nerve terminals was purified from Torpedo electric organ using a large-scale procedure. Up to 500 g of frozen electric organ were fractioned in a single run, leading to the isolation of greater than 100 mg of PSPM proteins. The purity of the fraction is similar to that of the synaptosomal plasma membrane obtained after subfractionation of Torpedo synaptosomes as judged by its membrane-bound acetylcholinesterase activity, the number of Glycera convoluta neurotoxin binding sites, and the binding of two monoclonal antibodies directed against PSPM. The specificity of these antibodies for the PSPM is demonstrated by immunofluorescence microscopy. |
format | Text |
id | pubmed-2113949 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 1985 |
publisher | The Rockefeller University Press |
record_format | MEDLINE/PubMed |
spelling | pubmed-21139492008-05-01 Large-scale purification of presynaptic plasma membranes from Torpedo marmorata electric organ J Cell Biol Articles The presynaptic plasma membrane (PSPM) of cholinergic nerve terminals was purified from Torpedo electric organ using a large-scale procedure. Up to 500 g of frozen electric organ were fractioned in a single run, leading to the isolation of greater than 100 mg of PSPM proteins. The purity of the fraction is similar to that of the synaptosomal plasma membrane obtained after subfractionation of Torpedo synaptosomes as judged by its membrane-bound acetylcholinesterase activity, the number of Glycera convoluta neurotoxin binding sites, and the binding of two monoclonal antibodies directed against PSPM. The specificity of these antibodies for the PSPM is demonstrated by immunofluorescence microscopy. The Rockefeller University Press 1985-11-01 /pmc/articles/PMC2113949/ /pubmed/2997233 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 Large-scale purification of presynaptic plasma membranes from Torpedo marmorata electric organ |
title | Large-scale purification of presynaptic plasma membranes from Torpedo marmorata electric organ |
title_full | Large-scale purification of presynaptic plasma membranes from Torpedo marmorata electric organ |
title_fullStr | Large-scale purification of presynaptic plasma membranes from Torpedo marmorata electric organ |
title_full_unstemmed | Large-scale purification of presynaptic plasma membranes from Torpedo marmorata electric organ |
title_short | Large-scale purification of presynaptic plasma membranes from Torpedo marmorata electric organ |
title_sort | large-scale purification of presynaptic plasma membranes from torpedo marmorata electric organ |
topic | Articles |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2113949/ https://www.ncbi.nlm.nih.gov/pubmed/2997233 |