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- Blaschko H. The mechanism of catalase inhibitions. Biochem J. 1935 Oct;29(10):2303–2312. doi: 10.1042/bj0292303. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Brill A. S., Williams R. J. Primary compounds of catalase and peroxidase. Biochem J. 1961 Feb;78(2):253–262. doi: 10.1042/bj0780253. [DOI] [PMC free article] [PubMed] [Google Scholar]
- CHANCE B., SCHONBAUM G. R. The nature of the primary complex of catalase. J Biol Chem. 1962 Jul;237:2391–2395. [PubMed] [Google Scholar]
- CHANCE B. The effect of pH upon the equilibria of catalase compounds. J Biol Chem. 1952 Feb;194(2):483–496. [PubMed] [Google Scholar]
- CHANCE B. The reactions of catalase in the presence of the notatin system. Biochem J. 1950 Apr;46(4):387–402. doi: 10.1042/bj0460387. [DOI] [PMC free article] [PubMed] [Google Scholar]
- GEORGE P. The chemical nature of the second hydrogen peroxide compound formed by cytochrome c peroxidase and horseradish peroxidase. I. Titration with reducing agents. Biochem J. 1953 May;54(2):267–276. doi: 10.1042/bj0540267. [DOI] [PMC free article] [PubMed] [Google Scholar]
- George P. The effect of the peroxide concentration and other factors on the decomposition of hydrogen peroxide by catalase. Biochem J. 1949;44(2):197–205. doi: 10.1042/bj0440197. [DOI] [PMC free article] [PubMed] [Google Scholar]
- KEILIN D., HARTREE E. F. Catalase, peroxidase and metmyoglobin as catalysts of coupled peroxidatic reactions. Biochem J. 1955 Jun;60(2):310–325. doi: 10.1042/bj0600310. [DOI] [PMC free article] [PubMed] [Google Scholar]
- KEILIN D., HARTREE E. F. Purification of horse-radish peroxidase and comparison of its properties with those of catalase and methaemoglobin. Biochem J. 1951 Jun;49(1):88–104. doi: 10.1042/bj0490088. [DOI] [PMC free article] [PubMed] [Google Scholar]
- KEILIN D., HARTREE E. F. Reactions of methaemoglobin and catalase with peroxides and hydrogen donors. Nature. 1954 Apr 17;173(4407):720–723. doi: 10.1038/173720a0. [DOI] [PubMed] [Google Scholar]
- KEILIN D., NICHOLLS P. Reactions of catalase with hydrogen peroxide and hydrogen donors. Biochim Biophys Acta. 1958 Aug;29(2):302–307. doi: 10.1016/0006-3002(58)90189-6. [DOI] [PubMed] [Google Scholar]
- Keilin D., Hartree E. F. Properties of azide-catalase. Biochem J. 1945;39(2):148–157. doi: 10.1042/bj0390148. [DOI] [PMC free article] [PubMed] [Google Scholar]
- MAEHLY A. C. Complexes of bacterial catalase with peroxide, azide and carbon monoxide. Biochim Biophys Acta. 1961 Nov 25;54:132–144. doi: 10.1016/0006-3002(61)90946-5. [DOI] [PubMed] [Google Scholar]
- MARGOLIASH E., NOVOGRODSKY A., SCHEJTER A. Irreversible reaction of 3-amino-1:2:4-triazole and related inhibitors with the protein of catalase. Biochem J. 1960 Feb;74:339–348. doi: 10.1042/bj0740339. [DOI] [PMC free article] [PubMed] [Google Scholar]
- NICHOLLS P. Ferrous complexes in the catalase reaction. Experientia. 1963 Feb 15;19:80–82. doi: 10.1007/BF02148029. [DOI] [PubMed] [Google Scholar]
- NICHOLLS P. The action of anions on catalase peroxide compounds. Biochem J. 1961 Nov;81:365–374. doi: 10.1042/bj0810365. [DOI] [PMC free article] [PubMed] [Google Scholar]
- NICHOLLS P. The formation and properties of sulphmyoglobin and sulphcatalase. Biochem J. 1961 Nov;81:374–383. doi: 10.1042/bj0810374. [DOI] [PMC free article] [PubMed] [Google Scholar]
- NICHOLLS P. The reaction between aminotriazole and catalase. Biochim Biophys Acta. 1962 May 21;59:414–420. doi: 10.1016/0006-3002(62)90191-9. [DOI] [PubMed] [Google Scholar]
- NICHOLLS P. The reduction of catalase by azide and peroxides. Biochim Biophys Acta. 1962 Apr 9;58:386–388. doi: 10.1016/0006-3002(62)91036-3. [DOI] [PubMed] [Google Scholar]
- OGURA Y. Catalase activity at high concentration of hydrogen peroxide. Arch Biochem Biophys. 1955 Aug;57(2):288–300. doi: 10.1016/0003-9861(55)90291-5. [DOI] [PubMed] [Google Scholar]
- TAYLOR D. M., BLIGH P. H., DUGGAN M. H. The absorption of calcium, strontium, barium and radium from the gastrointestinal tract of the rat. Biochem J. 1962 Apr;83:25–29. doi: 10.1042/bj0830025. [DOI] [PMC free article] [PubMed] [Google Scholar]
- THEORELL H., EHRENBERG A. Magnetic properties of some peroxide compounds of myoglobin, peroxidase and catalase. Arch Biochem Biophys. 1952 Dec;41(2):442–461. [PubMed] [Google Scholar]
- WIESNER K. The reaction mechanism of catalase. Experientia. 1962 Mar 15;18:115–116. doi: 10.1007/BF02153844. [DOI] [PubMed] [Google Scholar]