Accession Number : AD0750111
Title : Brain Acetylcholinesterase: Solubilization and Partial Purification by Affinity Chromatography.
Descriptive Note : Technical rept. Mar-Sep 71,
Corporate Author : EDGEWOOD ARSENAL MD
Personal Author(s) : Yamamura,Henry I. ; Gardner,Tommy L. ; Reichard,Douglas W. ; Broomfield,Clarence A.
Report Date : SEP 1972
Pagination or Media Count : 24
Abstract : Guinea pig brain acetylcholinesterase was solubilized by addition of Triton X-100. Affinity chromatography was used to partially purify the solubilized enzyme. Two specific competitive inhibitors, para-carboxyphenyltrimethyl ammonium iodide and meta-carboxyphenyltrimethyl ammonium iodide, were synthesized. Sodium chloride, choline chloride, physostigmine, and pyridinium 2-aldoxime methiodide were used as eluants. Of the inhibitors synthesized, the meta-carboxyphenyltrimethyl ammonium iodide analog gave the better results. A sodium chloride elution followed by a linear gradient of choline chloride provided the best elution of the bound enzyme. The partially purified enzyme hydrolyzed 0.01 moles of 14C-acetylcholine per hour per milligram protein, a 1000-fold purification. (Author)
Descriptors : (*ACETYLCHOLINESTERASE, PURIFICATION), SOLUBILITY, CHROMATOGRAPHIC ANALYSIS, AMMONIUM COMPOUNDS, HYDROLYSIS, MOLECULAR ASSOCIATION, BRAIN
Subject Categories : Biochemistry
Distribution Statement : APPROVED FOR PUBLIC RELEASE