Steinberg_1990_Biochem.Int_21_1043

Reference

Title : Torpedo acetylcholinesterase is inactivated by thiol reagents - Steinberg_1990_Biochem.Int_21_1043
Author(s) : Steinberg N , Roth E , Silman I
Ref : Biochemistry International , 21 :1043 , 1990
Abstract :

A number of sulphydryl reagents inhibit AChE of Torpedo california with pseudo-first-order kinetics, and inhibition can be retarded by quaternary ligands which bind at either the catalytic or peripheral anionic binding sites. Colorimetric determination with one of the inhibitory sulphydryl agents, 5,5'-dithiobis (2-nitrobenzoic acid), reveals the presence of a single thiol group per catalytic subunit; our data thus suggest that inhibition is achieved by reaction with the single free sulphydryl group of Cys231.

PubMedSearch : Steinberg_1990_Biochem.Int_21_1043
PubMedID: 1964378

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Citations formats

Steinberg N, Roth E, Silman I (1990)
Torpedo acetylcholinesterase is inactivated by thiol reagents
Biochemistry International 21 :1043

Steinberg N, Roth E, Silman I (1990)
Biochemistry International 21 :1043