Studies on Butyrylcholinesterase Inhibitors.
Abstract
The ultimate object of the present studies is the elucidation of the structure, function, and physiological significance of the enzyme, butyryl-cholinesterase (BuChE, E.C.3.1.1.8). It occurs in the blood, tissues, ganglia and cytosol of organisms and cells (1,2,3), and its structure (4), substrate, and inhibitor patterns resemble those of acety/cholinesterase (AChE). Both enzymes possess many inhibitors in common, including organo-phosphate (OP) threat agents, but preferential inhibition of either enzyme frequently occurs. Among the compounds which preferentially suppress BuChE in comparison with AChE are those which exert significant neurophar-macological effects, for example, the phenothiazines, tropates, phencyclidines, butyrophenones, imipramines, and curariforms (1,5,6,7,8,9). Phenothiazines, butyrophenones and imipramines are tranquillizers, tropates are spasmodics, and phencyclidines are hallucinogens. BuChE inhibition relative to the pharmacologic or toxic influence of such drugs and threat agents is unknown, despite the overt medical importance these compounds possess. In addition, they possess unusual military significance, since phenothiazines and atropine, in particular, are frequently included in OP antidotal formulations (10,11). (Author)
Document Details
- Document Type
- Technical Report
- Publication Date
- Jun 18, 1982
- Accession Number
- ADA117474
Entities
People
- Alan D. Wolfe
- Clarence E. Emery
- Dorothy A. Prichard
- Jeff S. Verdier
Organizations
- Walter Reed Army Institute of Research