Studies on Phyto-peroxidase
- 1 February 1961
- journal article
- research article
- Published by Oxford University Press (OUP) in Agricultural and Biological Chemistry
- Vol. 25 (2) , 136-140
- https://doi.org/10.1080/00021369.1961.10857786
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 540 mμ, for the oxidized form and at 425 and 560 mμ 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.This publication has 3 references indexed in Scilit:
- Chromatography of Proteins. I. Cellulose Ion-exchange AdsorbentsJournal of the American Chemical Society, 1956
- Magnetic properties of some peroxide compounds of myoglobin, peroxidase and catalaseArchives of Biochemistry and Biophysics, 1952
- Purification of horse-radish peroxidase and comparison of its properties with those of catalase and methaemoglobinBiochemical Journal, 1951