[Adsorptive and catalytic properties of cholinesterase on phospholipid monolyers in different oxidation states]

Adsorption isotherm and enzymatic activity of protein interacting with the surface of solid carrier formed by oriented fat lipid chains of differently oxidized phospholipids have been studied. It has been found that the appearance of peroxide groups in fat acid chains results in a twofold decrease of protein limiting adsorption on the lipid monolayer. The data on enzymatic activity of proteins at variously filled suface with protein molecules indicate that the peroxide groups produce an activating effect under the conditions when protein interactions can be neglected. Superoxidation of phospholipid fat acids is suggested to be one of the mechanisms involved in the control of the processes proceeding on the membranes.