Accession Number : AD0696742

Title :   THE PROPERTIES OF ACETYLCHOLINESTERASE MODIFIED BY INTERACTION WITH THE ALKYLATING AGENT N,N-DIMETHYL-2-PHENYLAZIRIDINIUM ION,

Corporate Author : DEFENCE CHEMICAL BIOLOGICAL AND RADIATION ESTABLISHMENT OTTAWA (ONTARIO)

Personal Author(s) : Purdie,Jocelyn E.

Report Date : 13 JAN 1969

Pagination or Media Count : 13

Abstract : The interaction of N,N-dimethyl-2-phenylaziridinium ion with bovine erythrocyte acetylcholinesterase (acetylcholine hydrolase, EC 3.1.1.7) and the product of this interaction have been investigated in some detail. Initially DPA inhibits acetylcholinesterase towards the hydrolysis of acetylcholine and isoamyl acetate. With time, an irreversible reaction develops, resulting in a product with an activity greater or less than that of acetylcholinesterase, depending on the substrate. The product of the irreversible reaction (DPA-enzyme) has little or no affinity for compounds containing a quarternary nitrogen functions but has esteratic activity towards uncharged esters. Compared with acetylcholinesterase it demonstrates considerably less substrate specificity as shown by its behaviour towards a series of aliphatic acetates (ranging from ethyl to 3,3-dimethylbutyl) and towards a series of para-substituted phenylacetates. It is also characterized by uniformly low k(cat) values. This is tentatively interpreted as resulting from difficulty in deacetylation. (Author)

Descriptors :   (*ACETYLCHOLINESTERASE, CHEMICAL REACTIONS), AMMONIUM COMPOUNDS, NITROGEN HETEROCYCLIC COMPOUNDS, CANADA

Subject Categories : Biochemistry

Distribution Statement : APPROVED FOR PUBLIC RELEASE