In:
Zeitschrift für Naturforschung C, Walter de Gruyter GmbH, Vol. 73, No. 9-10 ( 2018-09-25), p. 345-351
Abstract:
The dependence of the activity of acetylcholinesterase from electric eel at a pH value range of 4.8–9.8 (phosphate buffer), regarding acetylcholine and acetylthiocholine hydrolysis, was determined at 25 °C, ionic strength of 0.11 M, and initial substrate concentration of 4 mM. At a pH range of 4.8–9.8, the dependences A (pH) form a sigmoid increasing curve with the maximum catalytic activity at a pH range 8–9.5. For acetylcholine hydrolysis, the kinetic reason for such an increase in A consists mainly of an increase in the rate constant k 2 (Michaelis-Menten) model with increasing pH of the reaction mixture. For acetylthiocholine hydrolysis, the kinetic explication of the determined dependence A (pH) is more complicated.
Type of Medium:
Online Resource
ISSN:
1865-7125
,
0939-5075
DOI:
10.1515/znc-2017-0134
Language:
English
Publisher:
Walter de Gruyter GmbH
Publication Date:
2018
detail.hit.zdb_id:
2078107-6
SSG:
12