An anion-exchange resin, Amberlite IRA 900 modified with manganese-tetrakis(sulfophenyl)porphine (MnTPPSr), was used in place of peroxidase for the determination of hydrogen peroxide by the following enzyme-reaction: 2H2O2+phenol+4-aminoantipyrine pero-x' quinoid dye(2mpx=505 nm)+4H2O. The calibration curve was linear in the range from 5 µg to 50 µg of hydrogen peroxide with a relative standard deviation of 1.05% (n=10). The absorbance of the quinoid dye formed by the use of Mn-TPPSr reached approximately 80% of that obtained by the control peroxidase method. The activity of MnTPPSr did not deteriorate over repeated uses. Only slight interferences of foreign substances were found except for the case of ascorbic acid.
In an attempt to develop a practically useful mimesis of peroxidase, the peroxidase-like catalytic activity of anion exchange resins (Amberlite IRA 900) modified with manganese, cobalt, iron, copper and zinc complexes of some porphyrins was examined in terms of the accelerating effect on dye formation in the following reaction. The evaluation of the activity was carried out by comparison of the effect obtained by using the resins with that obtained by using peroxidase. In the previous paper,1) the peroxidase-like catalytic activity of anion-exchange resins modified with metalloporphyrins in the dye formation of phenol with 4-aminoantipyrine (AAP) by hydrogen peroxide was reported. Amberlite IRA 900 modified with manganesetetrakis(sulfophenyl)porphine (MnTPPSr) was found to be useful in the determination of hydrogen peroxide by the use of these chromogens.2) However, in this color reaction, a large excess of phenol was necessary to obtain a good result, because phenol and the dye formed were adsorbed by the resin. Accordingly, we consider that it is more advantageous to use N,Ndiethylaniline (DEA) which is a kind of base, as a chromogen in place of phenol (see the reaction in Fig. 1
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