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Vopr Med Khim ; 21(4): 396-400, 1975.
Article in Russian | MEDLINE | ID: mdl-175565

ABSTRACT

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".


Subject(s)
Carboxy-Lyases/metabolism , Histidine Decarboxylase/metabolism , Binding Sites , Gels , Histidine , Imidazoles/pharmacology , Micrococcus/enzymology , Protein Binding , Silicon Dioxide
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