On the Mechanism of Peroxidase Catalyzed Oxidations Studied by Means of Chemiluminescence Measurements.
- 1 January 1964
- journal article
- research article
- Published by Danish Chemical Society in Acta Chemica Scandinavica
- Vol. 18 (2) , 389-401
- https://doi.org/10.3891/acta.chem.scand.18-0389
Abstract
The enzymic oxidation of pyrogallol is accompanied by chemiiuminescence, the measurement of which provides a sensitive and useful assay method for peroxidatic activity of purified as well as for crude enzyme preparations. The present investigation is concerned with the characterization and kinetics of the luminescent species involved in this reaction.This publication has 8 references indexed in Scilit:
- Identification, by Electron Paramagnetic Resonance Spectroscopy, of Free Radicals Generated from Substrates by PeroxidaseJournal of Biological Chemistry, 1960
- THE THIRD INTERMEDIATE COMPOUND OF HORSERADISH PEROXIDASE AND HYDROGEN PEROXIDEJournal of Biological Chemistry, 1953
- The transition from the primary to the secondary peroxidase-peroxide complexArchives of Biochemistry and Biophysics, 1952
- Purification of horse-radish peroxidase and comparison of its properties with those of catalase and methaemoglobinBiochemical Journal, 1951
- THE PROPERTIES OF THE ENZYME-SUBSTRATE COMPOUNDS OF HORSERADISH PEROXIDASE AND PEROXIDES .3. THE REACTION OF COMPLEX-II WITH ASCORBIC ACID1949
- THE ENZYME-SUBSTRATE COMPOUNDS OF HORSERADISH PEROXIDASE AND PEROXIDES .2. KINETICS OF FORMATION AND DECOMPOSITION OF THE PRIMARY AND SECONDARY COMPLEXES1949
- On the haematin compound of peroxidaseProceedings of the Royal Society of London. B. Biological Sciences, 1937
- The kinetics of peroxidase actionBiochemical Journal, 1931