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Electrophorus acetylcholinesterase. Biochemical and electron microscope characterization of low ionic strength aggregates
The "tailed" molecules of Electrophorus (electric eel) acetylcholinesterase aggregate under conditions of low ionic strength. These aggregates have been studied by sedimentation analysis and high- resolution electron microscopy. They consist of bundles of at least half a dozen molecules, t...
Formato: | Texto |
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Lenguaje: | English |
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The Rockefeller University Press
1978
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Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2110035/ https://www.ncbi.nlm.nih.gov/pubmed/649654 |
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collection | PubMed |
description | The "tailed" molecules of Electrophorus (electric eel) acetylcholinesterase aggregate under conditions of low ionic strength. These aggregates have been studied by sedimentation analysis and high- resolution electron microscopy. They consist of bundles of at least half a dozen molecules, the tails of which are packed side by side, to form the core of the structure. Although aggregation is normally fully reversible, aggregates were irreversibly stabilized by methylene blue- sensitized photo-oxidation. This process was shown to consist of a singlet oxygen oxidation reaction and probably involves methionine or histidine residues. It did not modify the structural or hydrodynamic characteristics of the aggregates. |
format | Text |
id | pubmed-2110035 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 1978 |
publisher | The Rockefeller University Press |
record_format | MEDLINE/PubMed |
spelling | pubmed-21100352008-05-01 Electrophorus acetylcholinesterase. Biochemical and electron microscope characterization of low ionic strength aggregates J Cell Biol Articles The "tailed" molecules of Electrophorus (electric eel) acetylcholinesterase aggregate under conditions of low ionic strength. These aggregates have been studied by sedimentation analysis and high- resolution electron microscopy. They consist of bundles of at least half a dozen molecules, the tails of which are packed side by side, to form the core of the structure. Although aggregation is normally fully reversible, aggregates were irreversibly stabilized by methylene blue- sensitized photo-oxidation. This process was shown to consist of a singlet oxygen oxidation reaction and probably involves methionine or histidine residues. It did not modify the structural or hydrodynamic characteristics of the aggregates. The Rockefeller University Press 1978-05-01 /pmc/articles/PMC2110035/ /pubmed/649654 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 Electrophorus acetylcholinesterase. Biochemical and electron microscope characterization of low ionic strength aggregates |
title | Electrophorus acetylcholinesterase. Biochemical and electron microscope characterization of low ionic strength aggregates |
title_full | Electrophorus acetylcholinesterase. Biochemical and electron microscope characterization of low ionic strength aggregates |
title_fullStr | Electrophorus acetylcholinesterase. Biochemical and electron microscope characterization of low ionic strength aggregates |
title_full_unstemmed | Electrophorus acetylcholinesterase. Biochemical and electron microscope characterization of low ionic strength aggregates |
title_short | Electrophorus acetylcholinesterase. Biochemical and electron microscope characterization of low ionic strength aggregates |
title_sort | electrophorus acetylcholinesterase. biochemical and electron microscope characterization of low ionic strength aggregates |
topic | Articles |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2110035/ https://www.ncbi.nlm.nih.gov/pubmed/649654 |