TURNIP PEROXIDASE: I. PURIFICATION AND PHYSICOCHEMICAL PROPERTIES OF MULTIPLE COMPONENTS IN TURNIP PEROXIDASE*
- 25 March 1960
- journal article
- research article
- Published by Oxford University Press (OUP) in The Journal of Biochemistry
- Vol. 47 (3) , 369-381
- https://doi.org/10.1093/oxfordjournals.jbchem.a127074
Abstract
The aqueous extract is fractionated with (NH4)2SO4 to the 0.3[long dash]0.5 and 0.5[long dash]0.8 saturation fractions. The latter is treated with 50% ethanol, and the filtrate is separated by starch zone electrophoresis to peroxidases A1 and A2. From the former (0.3.[long dash]0.5 saturation fraction) peroxidase D is precipitated by 50% ethanol. The prepns. A1, A2 and D show the following values: R.Z. 3.36, 3.73, and 2.46; mol. wt., 49000, 45000 and 43000, resp.; absorption bands at 276-278, 402-405, 494-499, and 642-643 m[mu]; P.Z., 340, 260 and 1200, resp. Besides them peroxidase prepn. B is partly purified and analyzed as horseradish peroxidase I-type, while the A1, A2 and D prepns. are the H-type.This publication has 4 references indexed in Scilit:
- Multiple components in horse-radish peroxidaseBiochemical Journal, 1954
- The chemical nature of the second hydrogen peroxide compound formed by cytochrome c peroxidase and horseradish peroxidase. 1. Titration with reducing agentsBiochemical Journal, 1953
- *EIN QUANTITATIVES VERFAHREN ZUR ANALYSE DER SERUMPROTEINE DURCH PAPIERELEKTROPHORESE1952
- Purification of horse-radish peroxidase and comparison of its properties with those of catalase and methaemoglobinBiochemical Journal, 1951