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CHOLINE ESTERASE AND THE THEORY OF CHEMICAL MEDIATION OF NERVE IMPULSES
The maximum choline esterase activity of the superior cervical ganglion of the cat was measured and found to be, on the average, equivalent to the splitting of 0.10γ of acetyl choline chloride per second per milligram of fresh tissue at a pH of 7.4 and 38°. The least possible time required for destr...
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Formato: | Texto |
Lenguaje: | English |
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The Rockefeller University Press
1938
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Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2141955/ https://www.ncbi.nlm.nih.gov/pubmed/19873059 |
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author | Glick, David |
author_facet | Glick, David |
author_sort | Glick, David |
collection | PubMed |
description | The maximum choline esterase activity of the superior cervical ganglion of the cat was measured and found to be, on the average, equivalent to the splitting of 0.10γ of acetyl choline chloride per second per milligram of fresh tissue at a pH of 7.4 and 38°. The least possible time required for destruction of the ester liberated by one nerve impulse was calculated to be 0.015σ. The dissociation constant of the reaction between the enzyme and acetyl choline chloride was determined, and a value of 0.001 was obtained. From the value of the dissociation constant, the time for hydrolysis at the minimum rate was calculated to be about 8 seconds. It was shown that a localization of enzyme and substrate within the ganglion cell would have to exist in order that enzymatic destruction of acetyl choline liberated by nerve impulses occur within the span of the refractory period. |
format | Text |
id | pubmed-2141955 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 1938 |
publisher | The Rockefeller University Press |
record_format | MEDLINE/PubMed |
spelling | pubmed-21419552008-04-23 CHOLINE ESTERASE AND THE THEORY OF CHEMICAL MEDIATION OF NERVE IMPULSES Glick, David J Gen Physiol Article The maximum choline esterase activity of the superior cervical ganglion of the cat was measured and found to be, on the average, equivalent to the splitting of 0.10γ of acetyl choline chloride per second per milligram of fresh tissue at a pH of 7.4 and 38°. The least possible time required for destruction of the ester liberated by one nerve impulse was calculated to be 0.015σ. The dissociation constant of the reaction between the enzyme and acetyl choline chloride was determined, and a value of 0.001 was obtained. From the value of the dissociation constant, the time for hydrolysis at the minimum rate was calculated to be about 8 seconds. It was shown that a localization of enzyme and substrate within the ganglion cell would have to exist in order that enzymatic destruction of acetyl choline liberated by nerve impulses occur within the span of the refractory period. The Rockefeller University Press 1938-03-20 /pmc/articles/PMC2141955/ /pubmed/19873059 Text en Copyright © Copyright, 1938, by The Rockefeller Institute for Medical Research 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 Glick, David CHOLINE ESTERASE AND THE THEORY OF CHEMICAL MEDIATION OF NERVE IMPULSES |
title | CHOLINE ESTERASE AND THE THEORY OF CHEMICAL MEDIATION OF NERVE IMPULSES |
title_full | CHOLINE ESTERASE AND THE THEORY OF CHEMICAL MEDIATION OF NERVE IMPULSES |
title_fullStr | CHOLINE ESTERASE AND THE THEORY OF CHEMICAL MEDIATION OF NERVE IMPULSES |
title_full_unstemmed | CHOLINE ESTERASE AND THE THEORY OF CHEMICAL MEDIATION OF NERVE IMPULSES |
title_short | CHOLINE ESTERASE AND THE THEORY OF CHEMICAL MEDIATION OF NERVE IMPULSES |
title_sort | choline esterase and the theory of chemical mediation of nerve impulses |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2141955/ https://www.ncbi.nlm.nih.gov/pubmed/19873059 |
work_keys_str_mv | AT glickdavid cholineesteraseandthetheoryofchemicalmediationofnerveimpulses |