[Effect of Polyakov's "prints" on the catalytic properties of an enzyme substrate system].

Silicagels, formed in presence of an enzyme (histidine decarboxylase from Micrococcus sp. n.), substrate (L-histidine-HCl-H2O) and inhibitor (imidazole) (so-called Polyakov's "print") exhibited specific catalytic properties in the reaction of L-histidine decarboxylation. The "prints" of the enzyme, inhibitor and substrate increased the activity of the enzyme-substrate system studied. The increased activity was probably due to the specific adsorption of imidazole ring of the substrate molecule by the "print".