Reaction of 3-amino-1:2:4-triazole with bovine liver catalase and human erythrocyte catalase |
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| Authors: | J Y Chang W A Schroeder |
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| Affiliation: | 1. Hammersmith Hospital, Imperial College Healthcare NHS Trust, London, United Kingdom;2. Centre for Haematology, Imperial College London, London, United Kingdom;1. Department of Internal Medicine, Yonsei University Wonju College of Medicine, Wonju, Republic of Korea;2. Institute of Lifestyle Medicine, Yonsei University Wonju College of Medicine, Wonju, Republic of Korea;3. Department of Internal Medicine, Soonchunhyang University Cheonan Hospital, Cheonan, Republic of Korea;4. Department of Preventive Medicine, Yonsei University Wonju College of Medicine, Wonju, Republic of Korea;5. Institute of Genomic Cohort, Yonsei University Wonju College of Medicine, Wonju, Republic of Korea |
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| Abstract: | The stoichiometry of the reaction of 3-amino-1:2:4-triazole with catalase is different for bovine liver and human erythrocyte catalases, and can be correlated with the hematin content of the two types of catalase. A specific histidyl residue in catalase is modified, but an intact hematin appears to be necessary for binding of hydrogen peroxide before reaction with aminotriazole can occur. |
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