Ionic strength dependence of the inhibition of acetylcholinesterase activity by Al3+

Thomas R. Sharp; Terrone L. Rosenberry

doi:10.1016/0301-4622(85)80013-2

Ionic strength dependence of the inhibition of acetylcholinesterase activity by Al³⁺

Thomas R. Sharp, Terrone L. Rosenberry

Neuroscience

Research output: Contribution to journal › Article › peer-review

7 Scopus citations

Abstract

Inhibition of acetylcholinesterase activity by Al³⁺ has been examined by initial velocity kinetics and by a first-order kinetic method. Both methods yield an inhibition constant of approx. 1.7 mM at 0.1 M ionic strength. The initial velocity study indicates a noncompetitive mechanism of inhibition by Al³⁺. Inhibition at 10 mM ionic strength shows a K_i of 0.03 mM. Evaluation of the ionic strength dependence concurs with the results of Nolte et al. (Biochemistry 19 (1980) 3705). An effective charge in the binding site of -9 predicts the ratio of inhibition constants at high and low ionic strength. Extrapolation to zero ionic strength gives a K_i⁰ = 0.34 μM.

Original language	English (US)
Pages (from-to)	261-264
Number of pages	4
Journal	Biophysical Chemistry
Volume	21
Issue number	3-4
DOIs	https://doi.org/10.1016/0301-4622(85)80013-2
State	Published - Mar 1985

Keywords

Acetylcholinesterase
Aluminum inhibition
Ionic strength dependence

ASJC Scopus subject areas

Biophysics
Biochemistry
Organic Chemistry

Access to Document

10.1016/0301-4622(85)80013-2

Cite this

@article{e166515ab19e4559b1bbaed2b8160a95,

title = "Ionic strength dependence of the inhibition of acetylcholinesterase activity by Al3+",

abstract = "Inhibition of acetylcholinesterase activity by Al3+ has been examined by initial velocity kinetics and by a first-order kinetic method. Both methods yield an inhibition constant of approx. 1.7 mM at 0.1 M ionic strength. The initial velocity study indicates a noncompetitive mechanism of inhibition by Al3+. Inhibition at 10 mM ionic strength shows a Ki of 0.03 mM. Evaluation of the ionic strength dependence concurs with the results of Nolte et al. (Biochemistry 19 (1980) 3705). An effective charge in the binding site of -9 predicts the ratio of inhibition constants at high and low ionic strength. Extrapolation to zero ionic strength gives a Ki0 = 0.34 μM.",

keywords = "Acetylcholinesterase, Aluminum inhibition, Ionic strength dependence",

author = "Sharp, {Thomas R.} and Rosenberry, {Terrone L.}",

note = "Funding Information: T.R.S. was a Postdoctoral Research Fellow of the Muscular Dystrophy Association of America. This work was supported by National Institutes of Health Grant NS 16577 and National Science Foundation Grant PCM 80-07061.T he technrcal assistance of Miss Lia Henke is acknowledged. Funds for constructing the computerized data acquisition/analysis system were provided by National Science Foundation Grant PCM 79-12001.",

year = "1985",

month = mar,

doi = "10.1016/0301-4622(85)80013-2",

language = "English (US)",

volume = "21",

pages = "261--264",

journal = "Biophysical Chemistry",

issn = "0301-4622",

publisher = "Elsevier",

number = "3-4",

}

TY - JOUR

T1 - Ionic strength dependence of the inhibition of acetylcholinesterase activity by Al3+

AU - Sharp, Thomas R.

AU - Rosenberry, Terrone L.

N1 - Funding Information: T.R.S. was a Postdoctoral Research Fellow of the Muscular Dystrophy Association of America. This work was supported by National Institutes of Health Grant NS 16577 and National Science Foundation Grant PCM 80-07061.T he technrcal assistance of Miss Lia Henke is acknowledged. Funds for constructing the computerized data acquisition/analysis system were provided by National Science Foundation Grant PCM 79-12001.

PY - 1985/3

Y1 - 1985/3

N2 - Inhibition of acetylcholinesterase activity by Al3+ has been examined by initial velocity kinetics and by a first-order kinetic method. Both methods yield an inhibition constant of approx. 1.7 mM at 0.1 M ionic strength. The initial velocity study indicates a noncompetitive mechanism of inhibition by Al3+. Inhibition at 10 mM ionic strength shows a Ki of 0.03 mM. Evaluation of the ionic strength dependence concurs with the results of Nolte et al. (Biochemistry 19 (1980) 3705). An effective charge in the binding site of -9 predicts the ratio of inhibition constants at high and low ionic strength. Extrapolation to zero ionic strength gives a Ki0 = 0.34 μM.

AB - Inhibition of acetylcholinesterase activity by Al3+ has been examined by initial velocity kinetics and by a first-order kinetic method. Both methods yield an inhibition constant of approx. 1.7 mM at 0.1 M ionic strength. The initial velocity study indicates a noncompetitive mechanism of inhibition by Al3+. Inhibition at 10 mM ionic strength shows a Ki of 0.03 mM. Evaluation of the ionic strength dependence concurs with the results of Nolte et al. (Biochemistry 19 (1980) 3705). An effective charge in the binding site of -9 predicts the ratio of inhibition constants at high and low ionic strength. Extrapolation to zero ionic strength gives a Ki0 = 0.34 μM.

KW - Acetylcholinesterase

KW - Aluminum inhibition

KW - Ionic strength dependence

UR - http://www.scopus.com/inward/record.url?scp=0021945555&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0021945555&partnerID=8YFLogxK

U2 - 10.1016/0301-4622(85)80013-2

DO - 10.1016/0301-4622(85)80013-2

M3 - Article

C2 - 3986284

AN - SCOPUS:0021945555

SN - 0301-4622

VL - 21

SP - 261

EP - 264

JO - Biophysical Chemistry

JF - Biophysical Chemistry

IS - 3-4

ER -