ON THE KINETICS OF THE HUMAN BLOOD CHOLINESTERASE
- 1 May 1956
- journal article
- research article
- Published by Oxford University Press (OUP) in The Journal of Biochemistry
- Vol. 43 (3), 315-326
- https://doi.org/10.1093/oxfordjournals.jbchem.a126632
Abstract
Serum cholinesterase and erythrocyte acetylcholinesterase are inhibited non-competitively by H+ and competitively by tetraethylammonium bromide. The latter inhibitor yields an inactive complex of the respective enzymes with the inhibitor (1 mol. to 1 mol.). The dissociation constant of the enzymes, and of enzyme-inhibitor compounds, and heat of ionization of the enzymes are calculated. The results are indicative of a single anionic site on the enzyme molecule.This publication has 11 references indexed in Scilit:
- The relationship of quaternary ammonium salts to the anionic sites of true and pseudo cholinesteraseBiochemical Journal, 1954
- THE ACTIVE SURFACE OF THE SERUM ESTERASEJournal of Biological Chemistry, 1954
- Quaternary ammonium salts as inhibitors of acetylcholine esteraseBiochimica et Biophysica Acta, 1952
- ON THE KINETICS OF THE HUMAN BLOOD CHOLINESTERASEThe Journal of Biochemistry, 1951
- Mechanism of enzymic hydrolysis I. Role of the acidic group in the estetratic site of acetylcholinesteraseBiochimica et Biophysica Acta, 1951
- The esterases of horse blood. 2. The specificity of horse erythrocyte cholinesteraseBiochemical Journal, 1950
- ACETYLCHOLINESTERASE .9. STRUCTURAL FEATURES DETERMINING THE INHIBITION BY AMINO ACIDS AND RELATED COMPOUNDS1950
- ACETYLCHOLINESTERASE .10. MECHANISM OF THE CATALYSIS OF ACYLATION REACTIONS1950
- ACETYLCHOLINESTERASE .8. DISSOCIATION CONSTANTS OF THE ACTIVE GROUPS1950
- THE REACTION OF ACETYLCHOLINE AND OTHER CARBOXYLIC ACID DERIVATIVES WITH HYDROXYLAMINE, AND ITS ANALYTICAL APPLICATIONJournal of Biological Chemistry, 1949