Distinct effect of xenobiotics on the metal-binding properties of protein molecules.

The X-ray standing-wave method was applied to study the elemental composition and molecular organization of ordered protein films of alkaline phosphatase exposed to different xenobiotics (drug compounds, lead). Binding of metal ions from triply distilled water to protein molecules has been experimentally observed. Definite differences in the arrangement of impurity metal ions in the films have been established.

[Enzyme immobilization on the dental enamel and its probable role in the physiology and pathology of the oral cavity].

Immobilized alkaline phosphatase was detected on the dental enamel surface of man by histochemical analysis for the first time. A heretofore unknown mechanism of the regulation of metabolic processes on the enamel-saliva border is discussed. Experimental findings confirm that irreversible absorption represent the immobilization mechanism.

[IR-spectroscopic study of lecithin and cholesterol layers adsorbed on Aerosil].

The IR-study of adsorbed layers of lecithin and cholesterol on aerosil was carried out. It was found that lipid molecules interact with adsorbent by means of hydrogen bonds with free surface hydroxyls. The structure of lipid layers on the surface of aerosil is discussed.

[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.