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Molecular Pharmacology, Vol 13, 283-290, Copyright © 1977 by the American Society for Pharmacology and Experimental Therapeutics

Drug Binding Properties of an agr-Bungarotoxin-Binding Component from Rat Brain

JAKOB SCHMIDT 1

1 Department of Biochemistry, State University of New York at Stony Brook, Stony Brook, New York 11794

The drug binding properties of an agr-bungarotoxin-binding component in a crude membrane preparation from whole rat brain were investigated by analyzing the effects of various neuroactive drugs on the rate of toxin binding. High affinities were found for nicotinic ligands such as d-tubocurarine, nicotine, gallamine, and dihydro-beta-erythroidine, whereas interaction with choline and muscarinic compounds was observed to be weak and presumably due to nonspecific electrostatic forces. Little interaction was seen with other putative neurotransmitters. No evidence was obtained for more than one type of toxin binding site. The findings are interpreted as supporting the notion that the agr-bungarotoxin-binding macromolecule in the central nervous system is a nicotinic acetylcholine receptor.

Note:
ACKNOWLEDGMENTS I gratefully acknowledge the expert technical assistance of Mrs. Indira Handy and the help of Mr. Joseph Lowy and Mr. Marshall Dawer in early phases of this work. beta-Nerve growth factor from mouse submaxillary glands was a gift of Dr. Alexander Wlodawer.

Submitted on June 28, 1976
Accepted on October 15, 1976




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C Romano and A Goldstein
Stereospecific nicotine receptors on rat brain membranes
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