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

Report Date:

1972-09-01

Pagination or Media Count:

24.0

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

Subject Categories:

  • Biochemistry

Distribution Statement:

APPROVED FOR PUBLIC RELEASE