[Role of acetylcholinesterase in the transmembrane transfer of anions in erythrocytes].

Data are presented in favour of the regulatory role of AChE in passive transmembrane transfer of anions: 1) gradual inhibition of the enzyme with proserin brings about the change of the transport activation energy and irregular shift of temperature in the salient point on Arrhenius curves; 2) complexing of different AChE inhibitors (succinyl cholinechlorine, tetraethyl ammonium, tetramethyl ammonium, d-tubocurarin, proserin) results in the change of transport velocity. A significant increase of membrane binding of highly efficient and specific inhibitor of SITS anion transport forming complexes with membrane transport sites under the effect of acetylcholine AChE substrate is recorded. Proserin acts in the same direction, but to a much lesser degree. The removal of acetylcholine effect which activates SITS binding with the AChE inhibitor points to the initiation of structural disturbances from this enzyme. The scheme of AChE regulatory effect is suggested: modification of the enzyme conformation at the interaction with the inhibitors or substrate--structural rearrangement of the membranes--modulation of anion channels.