[Comparative characteristics of acetylcholinesterase preparations from human erythrocytes with varying degrees of purity].

Preparations of human erythrocyte acetyl cholinesterase (HEACE) that differed in their specific activities (0.7 to 4.1 U/mg) and the final purification method were examined for protein and isoenzymic spectrum (by polyacrylamide gel disc electrophoresis), catalytic properties in the reaction of acetytriocholine hydrolysis, sensitivity to the specific organophosphorus inhibitor Gd-42, concentrations of active centres of HEACE, and activity of one catalytic centre. The preparations showed a stable spectrum of 11-12 proteins: HEACE had molecular heterogeneity and was electrophoretically separated into 3 fractions that differed in their aggregation level. Preparations with varying specific activity contained different HEACE quantities. Regardless of the purification degree, HEACE displayed similar activity of the catalytic centre and enzymic properties in reactions with the substrate and inhibitor.