[Isoenzymes of human blood cholinesterases and their genetic control].

Acetylcholinesterase from human erythrocytes solubilized by 1% Triton X-100 was resolved using polyacrylamide gel electrophoresis into two components. The first one (fast) is more firmly bound to cell membranes than the other. The existence of multiple forms (C1-C4) of serum cholinesterase-1 (CHE1) has been established. Electrophoresis in acid medium (pH 4.8) permits to detect the C5 component and a group of supplementary isoenzymes of cholinesterase-2. Individual differences observed in patterns of the CHE2 isozymes are controlled by a pair of autosomal codominant alleles Che2A and Che2B. The serum of subjects with phenotypes Che2AB(C5+) and Che2BB(C5-) showed on the average equal level of cholinesterase activity.