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Interaction and inhibition of acetylcholinesterase from Electrophorus electricus by nitrosamines.

Abstract：

:Kinetic analysis has shown that dimethylnitrosamine, dipropylnitrosamine, dibutylnitrosamine, and diphenylnitrosamine initially act as reversible competitive inhibitors with respect to the substrate, acetylthiocholine chloride. The inhibitor constants Ki vary from 21-30 microM for the aliphatic nitrosamines to 8.2 microM for the aromatic diphenylnitrosamine. With time they act as irreversible covalent inhibitors with dimethylnitrosamine producing 82% inactivation after 40 min. Pseudo-first-order kinetics are observed with the rate constant being proportional to the concentration of the nitrosamine and the order of reaction being equal to one. Fluorometry, gel chromatography, and equilibrium dialysis have been used to study the binding of the nitrosamines with acetylcholinesterase. Scatchard analysis indicates that dimethyl-, dipropyl-, and dibutylnitrosamine have a weaker affinity for the enzyme (Kd 5.6-8.08 microM) compared to diphenylnitrosamine (Kd 2.32 microM). In all cases the number of binding sites was four.

journal_name

Arch Biochem Biophys

journal_title

Archives of biochemistry and biophysics

authors

Shuttleworth B,de Villiers DL,Whiteley CG

doi

10.1016/0003-9861(90)90500-x

subject

Has Abstract

pub_date

1990-06-01 00:00:00

pages

338-44

issue

2

eissn

0003-9861

issn

1096-0384

pii

0003-9861(90)90500-X

journal_volume

279

pub_type

杂志文章

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