The DOI matches its Crossref record; 14 of the 14 references it cites were found in a registry or an index.
The steady-state kinetics of peroxidase with 2,2′-azino-di-(3-ethyl-benzthiazoline-6-sulphonic acid) as chromogen
Open accessAbstract
The chemical nature of the important new chromogen ABTS [2,2'-azino-di-(3-ethyl-benzthiazoline-6-sulphonic acid)] is described together with an account of the redox and spectroscopic properties of the system ABTS--H2O2--peroxidase. Keq. is calculated and a study of the steady-state kinetics over a whole range of substrate concentrations is reported. By using novel methods of kinetic analysis, an interpretation of the results is given which requires some extension of the classical peroxidase mechanism.
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Cites
Cleland, W. W. (1963) · Biochimica et Biophysica Acta · doi:10.1016/0006-3002(63)91800-6 · Cited by 2,088
Peroxidase Isozymes from Horseradish Roots
Shannon, L. M., Kay, E., & Lew, J. Y. (1966) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)96680-9 · Cited by 989
A new sensitive colorimetric assay for peroxidase using 3,3′-diaminobenzidine as hydrogen donor
Herzog, V., & Fahimi, H. D. (1973) · Analytical Biochemistry · doi:10.1016/0003-2697(73)90144-9 · Cited by 425
Interaction of Peroxidases with Aromatic Peracids and Alkyl Peroxides
Schonbaum, G. R., & Lo, S. (1972) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)45252-6 · Cited by 283
Ferdinand, W. (1966) · Biochemical Journal · doi:10.1042/bj0980278 · Cited by 199
Oxidation states of peroxidase
Yamazaki, I., & Yokota, K.-N. (1973) · Molecular and Cellular Biochemistry · doi:10.1007/bf01738677 · Cited by 170
Studies on the Equilibria and Kinetics of the Reactions of Peroxidase with Ligands
Wittenberg, J. B., Noble, R. W., Wittenberg, B. A., Antonini, E., Brunori, M., & Wyman, J. (1967) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)96250-2 · Cited by 165
The spectra of the enzyme-substrate complexes of catalase and peroxidase
Chance, B. (1952) · Archives of Biochemistry and Biophysics · doi:10.1016/0003-9861(52)90469-4 · Cited by 164
The oxidation of phenol and its reaction product by horseradish peroxidase and hydrogen peroxide
Danner, D. J., Brignac, P. J., Arceneaux, D., & Patel, V. (1973) · Archives of Biochemistry and Biophysics · doi:10.1016/0003-9861(73)90329-9 · Cited by 100
Reactions of the Oxyform of Horseradish Peroxidase
Tamura, M., & Yamazaki, I. (1972) · The Journal of Biochemistry · doi:10.1093/oxfordjournals.jbchem.a129768 · Cited by 83
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Khodaverdian, S., Dabirmanesh, B., Heydari, A., Dashtban-moghadam, E., Khajeh, K., & Ghazi, F. (2018) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2017.10.144 · Cited by 165
A method to measure antioxidant activity in organic media: Application to lipophilic vitamins
Cano, A., Acosta, M., & Arnao, M. B. (2000) · Redox Report · doi:10.1179/135100000101535933 · Cited by 156
Chen, C., Shrestha, R., Jia, K., Gao, P. F., Geisbrecht, B. V., Bossmann, S. H., Shi, J., & Li, P. (2015) · Journal of Biological Chemistry · doi:10.1074/jbc.m115.658807 · Cited by 124
Frog Skins Keep Redox Homeostasis by Antioxidant Peptides with Rapid Radical Scavenging Ability
Liu, C., Hong, J., Yang, H., Wu, J., Ma, D., Li, D., Lin, D., & Lai, R. (2010) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2010.01.036 · Cited by 97
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Metadata
- Authors
- Childs, R. E., & Bardsley, W. G.
- Venue
- Biochemical Journal
- Publisher
- Portland Press Ltd.
- Published
- 1975-01-01
- Volume
- 145
- Issue
- 1
- Pages
- 93-103
- ISSN
- 0264-6021 (ISSN-L)
- OpenAlex
- W1803620352
- Cited by
- 893
- References
- 14
- FWCI
- 8.90
- Type
- journal article
- Language
- en
- Open access
- bronze
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- CoChat. (2026). Citation check: The steady-state kinetics of peroxidase with 2,2′-azino-di-(3-ethyl-benzthiazoline-6-sulphonic acid) as chromogen. https://app.cochat.ai/papers/10.1042/bj1450093
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- Childs, R. E., & Bardsley, W. G. (1975). The steady-state kinetics of peroxidase with 2,2′-azino-di-(3-ethyl-benzthiazoline-6-sulphonic acid) as chromogen. Biochemical Journal. https://doi.org/10.1042/bj1450093
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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
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