THE EFFECT OF Cl − ON CHOLINE ACETYLTRANSFERASE KINETIC PARAMETERS AND A PROPOSED ROLE FOR Cl − IN THE REGULATION OF ACETYLCHOLINE SYNTHESIS

THE EFFECT OF Cl − ON CHOLINE ACETYLTRANSFERASE KINETIC PARAMETERS AND A PROPOSED ROLE FOR Cl... Abstract— Crude or purified rat brain choline acetyltransferase (ChAc) is activated by anions. Among anions, Cl− is the most effective and may promote an up to 60 fold increase in Vmax. In the absence of Cl−, at low ionic strength, acetylcholine (ACh) is a good ChAc inhibitor (Ki= 0.310 mm). The ACh inhibition becomes negligible when Cl− is increased to 145 mm (ACh Ki= 45 mm). These results are discussed in terms of regulation of ACh synthesis by nerve terminals. It is proposed that ChAc is part of a presynaptic membrane bound multienzymatic complex under direct control of the ion fluxes promoted by nerve impulses. http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Journal of Neurochemistry Wiley

THE EFFECT OF Cl − ON CHOLINE ACETYLTRANSFERASE KINETIC PARAMETERS AND A PROPOSED ROLE FOR Cl − IN THE REGULATION OF ACETYLCHOLINE SYNTHESIS

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Publisher
Wiley
Copyright
Copyright © 1977 Wiley Subscription Services, Inc., A Wiley Company
ISSN
0022-3042
eISSN
1471-4159
DOI
10.1111/j.1471-4159.1977.tb06504.x
Publisher site
See Article on Publisher Site

Abstract

Abstract— Crude or purified rat brain choline acetyltransferase (ChAc) is activated by anions. Among anions, Cl− is the most effective and may promote an up to 60 fold increase in Vmax. In the absence of Cl−, at low ionic strength, acetylcholine (ACh) is a good ChAc inhibitor (Ki= 0.310 mm). The ACh inhibition becomes negligible when Cl− is increased to 145 mm (ACh Ki= 45 mm). These results are discussed in terms of regulation of ACh synthesis by nerve terminals. It is proposed that ChAc is part of a presynaptic membrane bound multienzymatic complex under direct control of the ion fluxes promoted by nerve impulses.

Journal

Journal of NeurochemistryWiley

Published: Dec 1, 1977

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