title: [Purification of acetylcholinesterase from human erythrocytes using metal-chelate affinity chromatography].
abstract: Acetylcholinesterase (AChE) was purified on columns with iminodiacetate Agarose charged with Cu2+, Zn2+, and Ni2+. The best results (a 14-fold purification and more than 30% activity yield) were obtained with Zn2+ used as a complex-forming metal. The preparation had a specific activity of approximately 7 U. Its purity was tested by polyacrylamide gel electrophoresis under denaturing conditions.
authors.forename: A V
authors.initials: AV
authors.lastname: Il'ina
authors.forename: G E
authors.initials: GE
authors.lastname: Bannikova
authors.forename: V P
authors.initials: VP
authors.lastname: Varlamov
authors.forename: R S
authors.initials: RS
authors.lastname: Agabekian
mesh_terms: D000110:Acetylcholinesterase / Q000097:blood / Q000302:isolation & purification*; D002614:Chelating Agents / Q000737:chemistry; D002846:Chromatography, Affinity / Q000379:methods*; D004589:Electrophoresis, Disc; D004912:Erythrocytes / Q000201:enzymology*; D006801:Humans; D008670:Metals / Q000737:chemistry
chemical_list: D002614:Chelating Agents; D008670:Metals; D000110:Acetylcholinesterase