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CHOLINESTERASE IN DENERVATED END PLATES AND MUSCLE FIBRES

Parallel studies were made of cholinesterase activities and localizations in denervated rat and rabbit gastrocnemius muscle. Koelle's histochemical reaction was used for demonstrating the localization of cholinesterases. Enzyme activities in whole sliced muscle were measured by electrometric ti...

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Detalles Bibliográficos
Autores principales: Brzin, Miro, Majcen-Tkačev, Živa
Formato: Texto
Lenguaje:English
Publicado: The Rockefeller University Press 1963
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2106884/
https://www.ncbi.nlm.nih.gov/pubmed/14086761
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author Brzin, Miro
Majcen-Tkačev, Živa
author_facet Brzin, Miro
Majcen-Tkačev, Živa
author_sort Brzin, Miro
collection PubMed
description Parallel studies were made of cholinesterase activities and localizations in denervated rat and rabbit gastrocnemius muscle. Koelle's histochemical reaction was used for demonstrating the localization of cholinesterases. Enzyme activities in whole sliced muscle were measured by electrometric titration. The Cartesian ampulla-diver technique was used for cholinesterase activity determinations in end plate regions or in small pieces of the muscle fibre itself. No changes in the activity of cholinesterases (ChE) were found in the whole denervated muscle which would account for its chemical supersensitivity. The ChE distribution pattern was changed so that the end plate region became less active in the denervated muscle than in the normal one. The decrease in ChE activity in the end plates seems to be largely compensated for by an increase of this enzyme elsewhere in the muscle. A possible connection between the spatial spread of cholinesterase activity and the enlargement of the acetylcholine-sensitive surface is discussed.
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spelling pubmed-21068842008-05-01 CHOLINESTERASE IN DENERVATED END PLATES AND MUSCLE FIBRES Brzin, Miro Majcen-Tkačev, Živa J Cell Biol Article Parallel studies were made of cholinesterase activities and localizations in denervated rat and rabbit gastrocnemius muscle. Koelle's histochemical reaction was used for demonstrating the localization of cholinesterases. Enzyme activities in whole sliced muscle were measured by electrometric titration. The Cartesian ampulla-diver technique was used for cholinesterase activity determinations in end plate regions or in small pieces of the muscle fibre itself. No changes in the activity of cholinesterases (ChE) were found in the whole denervated muscle which would account for its chemical supersensitivity. The ChE distribution pattern was changed so that the end plate region became less active in the denervated muscle than in the normal one. The decrease in ChE activity in the end plates seems to be largely compensated for by an increase of this enzyme elsewhere in the muscle. A possible connection between the spatial spread of cholinesterase activity and the enlargement of the acetylcholine-sensitive surface is discussed. The Rockefeller University Press 1963-11-01 /pmc/articles/PMC2106884/ /pubmed/14086761 Text en Copyright © 1963 by The Rockefeller Institute Press 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 Article
Brzin, Miro
Majcen-Tkačev, Živa
CHOLINESTERASE IN DENERVATED END PLATES AND MUSCLE FIBRES
title CHOLINESTERASE IN DENERVATED END PLATES AND MUSCLE FIBRES
title_full CHOLINESTERASE IN DENERVATED END PLATES AND MUSCLE FIBRES
title_fullStr CHOLINESTERASE IN DENERVATED END PLATES AND MUSCLE FIBRES
title_full_unstemmed CHOLINESTERASE IN DENERVATED END PLATES AND MUSCLE FIBRES
title_short CHOLINESTERASE IN DENERVATED END PLATES AND MUSCLE FIBRES
title_sort cholinesterase in denervated end plates and muscle fibres
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2106884/
https://www.ncbi.nlm.nih.gov/pubmed/14086761
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