Skip to main content
Advertisement

Main menu

  • Home
  • Articles
    • Current Issue
    • Fast Forward
    • Latest Articles
    • Special Sections
    • Archive
  • Information
    • Instructions to Authors
    • Submit a Manuscript
    • FAQs
    • For Subscribers
    • Terms & Conditions of Use
    • Permissions
  • Editorial Board
  • Alerts
    • Alerts
    • RSS Feeds
  • Virtual Issues
  • Feedback
  • Submit
  • Other Publications
    • Drug Metabolism and Disposition
    • Journal of Pharmacology and Experimental Therapeutics
    • Molecular Pharmacology
    • Pharmacological Reviews
    • Pharmacology Research & Perspectives
    • ASPET

User menu

  • My alerts
  • Log in
  • My Cart

Search

  • Advanced search
Molecular Pharmacology
  • Other Publications
    • Drug Metabolism and Disposition
    • Journal of Pharmacology and Experimental Therapeutics
    • Molecular Pharmacology
    • Pharmacological Reviews
    • Pharmacology Research & Perspectives
    • ASPET
  • My alerts
  • Log in
  • My Cart
Molecular Pharmacology

Advanced Search

  • Home
  • Articles
    • Current Issue
    • Fast Forward
    • Latest Articles
    • Special Sections
    • Archive
  • Information
    • Instructions to Authors
    • Submit a Manuscript
    • FAQs
    • For Subscribers
    • Terms & Conditions of Use
    • Permissions
  • Editorial Board
  • Alerts
    • Alerts
    • RSS Feeds
  • Virtual Issues
  • Feedback
  • Submit
  • Visit molpharm on Facebook
  • Follow molpharm on Twitter
  • Follow molpharm on LinkedIn
Research ArticleArticles

Responses of Acetylcholinesterase from Torpedo marmorata to Salts and Curarizing Drugs

JEAN-PIERRE CHANGEUX
Molecular Pharmacology September 1966, 2 (5) 369-392;
JEAN-PIERRE CHANGEUX
Service de Biochimie Cellulaire, Institut Pasteur, Paris, France; Department of Biology, New York State University, Buffalo, New York, and Virus Laboratory, University of California, Berkeley, California
  • Find this author on Google Scholar
  • Find this author on PubMed
  • Search for this author on this site
  • Article
  • Info & Metrics
  • eLetters
  • PDF
Loading

Abstract

The structure and catalytic activity of acetylcholinesterase (Acetylcholine acetyl-hydrolase, EC 3.1.1.7) (AChE) from Torpedo marmorata depend upon the ionic strength, Γ/2, of the environment. The sedimentation coefficient of the enzyme is 14 S at Γ/2 = 0.3, but is polydisperse in the range of 10-80 S at Γ/2 = 0.003. The optimal velocity of the reaction catalyzed by AChE increases with ionic strength, while under the same conditions the affinity for the substrate and for several reversible competitive inhibitors decreases. The relative decrease of affinity as a consequence of increased ionic strength is higher for inhibitor molecules containing two quaternary ammonium ions than for compounds containing a single quaternary ammonium group. Among the monoquaternary inhibitors, this decrease is greater for phenyltrimethylammonium than for its 3-hydroxy analog.

In solutions of low salt concentration (Γ/2 = 0.003) significant affinity of the enzyme for two pachycurares, flaxedil and d-tubocurarine, can be demonstrated. Both compounds produce partial inhibition of AChE activity, antagonize its inhibition by reversible competitive inhibitors including some leptocurares, and enhance the inhibition by 3-hydroxyphenyltrimethylammonium. By measuring the degree of protection of AChE against thermal inactivation, the dissociation constant for the flaxedil-enzyme complex can be estimated to be about 3 x 10-7 M.

These observations and their possible physiological significance are interpreted in terms of conformational alterations of the AChE molecule in response to the binding of the pharmacologic agents.

ACKNOWLEDGMENTS The author is greatly indebted to Dr. France Tazieff-Depierre for her contributions to the early stages of this research and gifts of most of the pharmacologic agents and to Mrs. Merry Rubin for her extensive assistance in the preparation of the manuscript. He thanks Drs. P. Ascher, R. Couteaux, J. C. Gerhart, and J. Monod for their comments and suggestions after reading the manuscript. This investigation was supported in part by grants from the National Institutes of Health, National Science Foundation, Jane Coffin Childs Memorial Fund, Délégation Générale à la Recherche Scientifique et Technique, and U.S. Public Health Service research grant GM 12159 from the National Institutes of General Medical Sciences. A portion of the research was carried out during tenure of an Eleanor Roosevelt International Cancer Fellowship administered by the International Union Against Cancer.

  • Copyright ©, 1966, by Academic Press Inc.

MolPharm articles become freely available 12 months after publication, and remain freely available for 5 years. 

Non-open access articles that fall outside this five year window are available only to institutional subscribers and current ASPET members, or through the article purchase feature at the bottom of the page. 

 

  • Click here for information on institutional subscriptions.
  • Click here for information on individual ASPET membership.

 

Log in using your username and password

Forgot your user name or password?

Purchase access

You may purchase access to this article. This will require you to create an account if you don't already have one.
PreviousNext
Back to top

In this issue

Molecular Pharmacology
Vol. 2, Issue 5
1 Sep 1966
  • Table of Contents
  • Table of Contents (PDF)
  • Index by author
  • Editorial Board (PDF)
Download PDF
Article Alerts
Sign In to Email Alerts with your Email Address
Email Article

Thank you for sharing this Molecular Pharmacology article.

NOTE: We request your email address only to inform the recipient that it was you who recommended this article, and that it is not junk mail. We do not retain these email addresses.

Enter multiple addresses on separate lines or separate them with commas.
Responses of Acetylcholinesterase from Torpedo marmorata to Salts and Curarizing Drugs
(Your Name) has forwarded a page to you from Molecular Pharmacology
(Your Name) thought you would be interested in this article in Molecular Pharmacology.
CAPTCHA
This question is for testing whether or not you are a human visitor and to prevent automated spam submissions.
Citation Tools
Research ArticleArticles

Responses of Acetylcholinesterase from Torpedo marmorata to Salts and Curarizing Drugs

JEAN-PIERRE CHANGEUX
Molecular Pharmacology September 1, 1966, 2 (5) 369-392;

Citation Manager Formats

  • BibTeX
  • Bookends
  • EasyBib
  • EndNote (tagged)
  • EndNote 8 (xml)
  • Medlars
  • Mendeley
  • Papers
  • RefWorks Tagged
  • Ref Manager
  • RIS
  • Zotero

Share
Research ArticleArticles

Responses of Acetylcholinesterase from Torpedo marmorata to Salts and Curarizing Drugs

JEAN-PIERRE CHANGEUX
Molecular Pharmacology September 1, 1966, 2 (5) 369-392;
del.icio.us logo Digg logo Reddit logo Twitter logo Facebook logo Google logo Mendeley logo
  • Tweet Widget
  • Facebook Like
  • Google Plus One

Jump to section

  • Article
  • Info & Metrics
  • eLetters
  • PDF

Related Articles

Cited By...

More in this TOC Section

Articles

  • Identification of ERα/β Heterodimer Selective Ligands
  • CAR ameliorates AKI-induced liver injury
  • Selectivity and Cysteine Dependence of RGS Inhibitors
Show more Articles

Article

  • Identification of ERα/β Heterodimer Selective Ligands
  • CAR ameliorates AKI-induced liver injury
  • Selectivity and Cysteine Dependence of RGS Inhibitors
Show more Article

Similar Articles

Advertisement
  • Home
  • Alerts
Facebook   Twitter   LinkedIn   RSS

Navigate

  • Current Issue
  • Fast Forward by date
  • Fast Forward by section
  • Latest Articles
  • Archive
  • Search for Articles
  • Feedback
  • ASPET

More Information

  • About Molecular Pharmacology
  • Editorial Board
  • Instructions to Authors
  • Submit a Manuscript
  • Customized Alerts
  • RSS Feeds
  • Subscriptions
  • Permissions
  • Terms & Conditions of Use

ASPET's Other Journals

  • Drug Metabolism and Disposition
  • Journal of Pharmacology and Experimental Therapeutics
  • Pharmacological Reviews
  • Pharmacology Research & Perspectives
ISSN 1521-0111 (Online)

Copyright © 2023 by the American Society for Pharmacology and Experimental Therapeutics