Studies on Phyto-peroxidase

Part XIII. Crystallization of Japanese-radish Peroxidase c

Abstract

Peroxidase c was isolated and purified from Japanese-radish roots by means of a chromatographic technique with carboxymethyl cellulose. Two or more components exhibiting the absorption spectrum of peroxidase c were separated chromatographically, and the most basic component was crystallized from ammonium sulphate solution. The Reinheit Zahl and the purpurogallin number of the crystalline preparation were found to be 3.55 and 1100 respectively. The absorption maxima were found at 420 and 540mμ for the oxidized form and at 425 and 560mμ for the reduced form. The crystalline preparation contained 1.57% protohematin as the prosthetic group, and then the minimum molecular weight of peroxidase c was found to be 41500.