Peroxidase-catalyzed oxidation of amines in the presence of phenols is a basic problem of great importance in catalysis [1]. Its applied significance is due to the extensive use of horseradish peroxidase (HRP) and its chromogenic reducing substrates-2,2'-azino-di-(3-ethyl-2,3-dihydrobenzthiazoline-6-sulfonate) (ABTS), o -phenylenediamine (OPD), and 3,3',5,5'-tetramethylbenzidine (TMB)-in enzyme immunoassays (EIAs) of a variety of biologically relevant antigens [2]. Largescale automated EIAs require stop-reagents capable of terminating peroxidase-catalyzed oxidation of chromogenic substrates. Systematic kinetic studies of peroxidase-catalyzed oxidation of TMB and OPD in the presence of phenols have been conducted in our laboratory over the last 15 years [1,3]. We were able to demonstrate that peroxidase-catalyzed oxidation of TMB is inhibited (with variable efficiency) by gallic acid and its polydisulfide (GAPDS) [4-6]; 2-amino-4-nitrophenol and its polydisulfide [7,8]; 1-amino-2-naphthole-4-sulfonate and its polydisulfide [9]; 2,4-dinitrosoresorcinol and polydisulfides of resorcinol and 2,4-dinitroresorcinol [10]; 3-aminophenol polydisulfide [11]; and propyl gallate (PG) [12]. Peroxidase-catalyzed oxidation of OPD was inhibited by GAPDS [5] and 1-amino-2-naphthole-4-sulfonate polydisulfide [9].Oxidation of TMB or OPD in combination with a substituted phenol or polyphenol was characterized quantitatively by two characteristics: the constant of inhibition ( K i ) and the stoichiometric inhibition factor ( f ), the latter being equal to the number of free radicals extinguished per molecule of an inhibitor [1, 3-12]. The highest inhibitory activity was exhibited by resorcinol polydisulfide (RPDS) ( K i = 0.78 µ M; f = 76) [10] and GAPDS ( K i = 1.33 µ M; f = 36) [5, 6], which may be used for complete termination of peroxidase-catalyzed TMB oxidation in the course of EIAs of various antigens. In practice, EIAs and tests of total antioxidant activity (TAA) assume minimal interactions of the phenol component with proteins of the mixtures analyzed.Dissociation of gallic acid and GAPDS at pH 7 and higher is viewed as their drawback, because it results in efficient interactions of GAPDS with enzymes and proteins of the mixtures analyzed [13]. It is therefore important to study the inhibition of amine oxidation by PG and PGPDS, which fail to dissociate at pH > 4.4 (for GA, pK = 4.41 [13]).In this work, we aimed at studying the kinetics and parameters of inhibition of peroxidase-catalyzed oxidation of ABTS and OPD by PG and PGPDS, with a view for their future use as stop-reagents in EIAs or as optimum calibrating inhibitors in test systems for measuring TAA in human and animal biological fluids; aminephenol pairs are widely used for quantitating TAA (based on its comparison with the antiradical activity of a calibrator).Abstract -Peroxidase-catalyzed oxidation of 2,2'-azino-di-(3-ethyl-2,3-dihydrobenzthiazoline-6-sulfonate) (ABTS) was competitively inhibited by propyl gallate (PG) and its polydisulfide (PGPDS) at 20 ° C in 0...