The Behavior of Horseradish Peroxidase at High Hydrogen Peroxide Concentrations*
- 1 June 1966
- journal article
- research article
- Published by American Chemical Society (ACS) in Biochemistry
- Vol. 5 (6), 2003-2008
- https://doi.org/10.1021/bi00870a031
Abstract
No abstract availableThis publication has 10 references indexed in Scilit:
- An Electron Spin Resonance Study of Some HemoproteinsJournal of Biological Chemistry, 1965
- INVESTIGATIONS ON MULTIPLE COMPONENTS OF COMMERCIAL HORSERADISH PEROXIDASE1965
- The role of the protein in haem enzymesBiochimica et Biophysica Acta, 1962
- CREVICE STRUCTURES IN HEMOPROTEIN REACTIONSProceedings of the National Academy of Sciences, 1958
- The chemical nature of the second hydrogen peroxide compound formed by cytochrome c peroxidase and horseradish peroxidase. 1. Titration with reducing agentsBiochemical Journal, 1953
- The kinetics and stoichiometry of the transition from the primary to the secondary peroxidase peroxide complexesArchives of Biochemistry and Biophysics, 1952
- The spectra of the enzyme-substrate complexes of catalase and peroxidaseArchives of Biochemistry and Biophysics, 1952
- Purification of horse-radish peroxidase and comparison of its properties with those of catalase and methaemoglobinBiochemical Journal, 1951
- Studies in peroxidase action. 4. The oxidation of 4-methoxy-2:6-dimethylaniline. Suggestions for a mechanismBiochemical Journal, 1950
- THE PROPERTIES OF THE ENZYME-SUBSTRATE COMPOUNDS OF PEROXIDASE AND PEROXIDES .1. THE SPECTRA OF THE PRIMARY AND SECONDARY COMPLEXES1949