Croatica Chemica Acta, Vol. 47 No. 3, 1975.
Izlaganje sa skupa
Inhibition of Acetylcholinesterase by N-Alkylpyridinium and N-Alkylpyridinium-2-aldoxime Salts
L. P. A. de Jong
; Chemical Laboratory TNO, Rijswijk (Z. H .), The Netherlands
G. Z. Wolring
; Chemical Laboratory TNO, Rijswijk (Z. H .), The Netherlands
Sažetak
The interaction of a series of N-a1kylpyridinium and N-alkylpyridinium-
2-aldoxime salts with bovine erythrocyte acetylcholinesterase
was investigated for inhibition of the hydrolysis of the
substrates acetylcholine and dimethylaminoethyl acetate.
The compounds cause a mixed inhibition of the acetylcholine
hydrolysis which is interpreted as an interaction with the free
enzyme (competitive component) and with the acetylenzyme (non-
competitive component). The results suggest that the compounds
have a higher affinity for the free enzyme than for the acetyl-
enzyme. Enlargement of the alkyl-group increases the binding
capacity to the free enzyme. The aldoxime group hardly effects the binding to the free enzyme, but tends to increase the binding to the acetyl-enzyme. Some results obtained with dimethylaminoethyl acetate support the mechanism of inhibition as proposed from acetylcholine hydrolysis inhibition. In contrast to this mechanism some compounds
do not influence or even increase the maximum velocity of the
dimethylaminoethyl acetate hydrolysis. It is suggested that a ternary
complex of enzyme, substrate and pyridinium compound may
be formed from which, in case of dimethylaminoethyl acetate, the
enzyme is more rapidly acetylated.
Ključne riječi
Hrčak ID:
196621
URI
Datum izdavanja:
3.12.1975.
Posjeta: 613 *