Milk peroxidase

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Abstract
The enzyme was prepared by fractional precipitation with (NH4)2SO4. The activity decreased very slowly at 0-5[degree] C. The enzyme was active at pH 4-10. A method of estimating H2O2 is described. The presence of proteins, phosphate, and H2SO4 influenced the volume of gas obtained. Conditions were devised by which nitrite was quantitatively oxidized by H2O2 with peroxidase. Tyrosine and trypto-phane were oxidized to colored products under similar conditions. Dihydroxyacetone and phenylglyoxal were oxidized by very dilute H2O2 without peroxidase. Cys-teine, glutathione and denatured proteins containing the -SH group interfere with tests for peroxidase with benzidine, guaiacum and to some extent with p-phenylenedi-amine.

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