MODIFICATION OF THE ESTERATIC ACTIVITY OF ACETYLCHOLINESTERASE BY ALKYLATION WITH 1,1-DIMETHYL-2-PHENYLAZIRIDINIUM ION

Authors
  1. Purdie, J.E.
  2. McIvor, R.A.
Corporate Authors
Defence Chemical Biological and Radiation Labs, Ottawa ONT (CAN)
Abstract
We have examined the behaviour of acetylcholinesterase irreversibly inhibited by DPA (DPA-enzyme) towards a number of substrates, and towards organophosphorus reagents. Although our results are consistent with the reaction of DPA at the anionic site(s), they are also not inconsistent with the alkylation of group(s) in the vicinity of site(s).
Report Number
DCBRL-500 — Reprint; Previously catalogued as DSIS 67-03692
Date of publication
15 Sep 1966
Number of Pages
5
Reprinted from
Biochimica et Biophysica Acta, vol 128, 1966, p 590-593
DSTKIM No
89-01238
CANDIS No
59170
Format(s):
Hardcopy;Originator's fiche received by DSIS

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