[Composition and various properties of acetylcholinesterase from human erythrocytes].

Composition and some properties of human erythrocyte acetylcholinesterase prepared for use in medical practice were studied. After electrophoresis 5 protein bands, two of which exhibited the enzymatic activity, were detected in the preparation. Three isoenzyme forms of acetylcholinesterase, dissimilar in their electrophoretic mobility, were detected in the preparation by ion exchange chromatography on DEAE Sephadex A-50.

[Properties of cholinesterase preparations from human erythroyctes].

A modified method is described for isolation of acetylcholinesterase from human erythrocytes using an additional step of gel filtration on Sephadex G-75. Preparations of acetylcholinesterase were liberated from thromaboplastic activity and their specific activity was increased due to removal of low molecular proteins and of the products of destruction of hemoglobin. Content of A and B isoantigens in the preparations obtained was rather low and content of hemoglobin, combined with other proteins in the form of oxyhemoglobin, did not exceed 12% of the total protein.

[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.

[Effect of Triton X-100 on properties of acetylcholinesterase from human erythrocytes].

The effect of Triton X-100 on catalytic properties of acetylcholinesterase from human erythrocytes under acetylcholine hydrolysis, on sensitivity of acetylcholinesterase to specific phosphoorganic inhibitors and eserine, and on the mobility and isoenyme spectrum under analytical electrophoresis in polyacrylamide gel is investigated. Triton X-100, independently on its concentration within 0.05-1.