[Interaction of membrane-bound and solubilized erythrocyte acetylcholinesterase with carbamates].

Physostigmine and neostigmine methylsulphate are shown to be the most strong inhibitors of acetylcholine esterase of human erythrocytes. The action of baigon is less pronounced and pyrimor is characterized as the weakest inhibitor. No differences are found between the membrane-bound and solubilized acetylcholine esterase relative to their ability to be inhibited by these carbamates. The preliminary treatment of acetylcholine esterase with carbamates protects the enzyme from the subsequent inhibition by the organophosphoric inhibitor. A higher concentration (1.6-2.1 times) of physostigmine and pyrimor and lower (1.7-1.9 times) one of baigon and neostigmine methylsulphate are needed for protection of the soluble enzyme than of the membrane-bound enzyme.