RT Journal Article
SR Electronic
T1 Purification and Fractionation of Acetylcholinesterase into Subspecies by Affinity Chromatography on a <em>d</em>-Tubocurarine—Sepharose Column
JF Molecular Pharmacology
JO Mol Pharmacol
FD American Society for Pharmacology and Experimental Therapeutics
SP 589
OP 593
VO 8
IS 5
A1 M. J. JUNG
A1 B. BELLEAU
YR 1972
UL http://molpharm.aspetjournals.org/content/8/5/589.abstract
AB A method is described for the covalent attachment of d-tubocurarine to Sepharose. The preparation was successfully used for the rapid purification of acetylcholinesterase by allosteric site affinity chromatography. Selective elution of the enzyme with NaCl solutions of various concentrations was readily achieved. Selective interference with adsorption by bisquaternary effectors, such as decamethonium, gave even better results. Of considerable interest was the observation that selective interference with adsorption of the enzyme on a tubocurarine-Sepharose column by β-D-methylsuccinyldicholine iodide led to complete separation into two subspecies in a ratio of approximately 1:1. ACKNOWLEDGMENTS The skillful assistance of Dr. T. Allen and Mrs. C. Jung was highly appreciated. The succinyldicholine analogues were prepared by Dr. E. Wülfert and Dr. J. Whiting of our laboratories.