Inaktivatsiia o-difenoloksidazy v protsesse reaktsii okisleniia pirokatekhina.

Translated title of the contribution: Inactivation of o-diphenoloxidase in the pyrocatechol oxidation reaction

I. A. Butovich, V. A. Tertykh

Research output: Contribution to journalArticle

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Abstract

The inactivation kinetics of o-diphenoloxidase isolated from potato tubers was studied in the process of pyrocatechol oxidation. The enzyme when saturated with the substrate is inactivated with the inactivation rate constant kin = 0.5-1.0 min-1; kin depends on the initial concentration of pyrocatechol. The ultimate yield of the enzymic reaction product increases linearly with the initial concentration of the enzyme. Introduction of ethylene-diaminosulphate, a substance which condenses with o-quinones, does not increase the operation stability of o-diphenoloxidase. The data obtained evidence for inactivation of o-diphenoloxidase either at the level of the enzyme-substrate complex or due to bimolecular reaction with the substrate.

Original languageRussian
Pages (from-to)527-532
Number of pages6
JournalUkrainskii biokhimicheskii zhurnal
Volume56
Issue number5
StatePublished - Sep 1 1984

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ASJC Scopus subject areas

  • Biochemistry

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