Simple spectrophotometric assay for measuring catalase activity in biological tissues
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The details of a precise, accurate, and sensitive spectrophotometric method for measuring catalase activity are presented here. The assay was established for biological samples and depends on the rapid formation of a stable and colored carbonato-cobaltate (III) complex. Samples exhibiting catalase activity are incubated with hydrogen peroxide solution for 2 min prior to rapid mixing of the incubation enzymatic reaction mixture with cobalt-bicarbonate reagent, which assesses non-reacting hydrogen peroxide. Catalase activity is always directly proportional to the rate of dissociation of hydrogen peroxide. Hydrogen peroxide acts to oxidize cobalt (II) to cobalt (III) in the presence of bicarbonate ions; this process ends with the production of a carbonato-cobaltate (III) complex ([Co (CO 3 ) 3 ]Co). The formed end product has two maximum absorbance peaks: 440 nm and 640 nm. The 440-nm peak has been utilized for assessing catalase activity. The catalase activity results of the current method for erythrocyte lysate homogenates were computationally identical to those of the dichromate method ( r = 0.9950). The coefficient of variation was calculated to determine the imprecision of the current assay. The within-run and between-run results were 2.96 and 3.83%, respectively. This method is appropriate for analyzing bacteria, red blood cells and liver and kidney tissue homogenates.
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Catalase activity in the studied system is conversely proportional to the obtained signal.
“Thus, the catalase activity in the studied system is conversely proportional to the obtained signal (Hadwan 2018).”
From Reactive Oxygen Species, Toxicity, Oxidative Stress, and Antioxidants: Chronic Diseases and Aging (2023) · cites this paper as Hadwan 2018
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- Authors
- Hadwan, M. H.
- Affiliations
- University of Babylon (IQ)
- Corresponding author
- Hadwan, Mahmoud Hussein
- Venue
- BMC Biochemistry
- Published
- 2018-08-03
- Volume
- 19
- Issue
- 1
- Pages
- 7-7
- ISSN
- 1471-2091 (ISSN-L)
- PMC
- PMC6091033
- OpenAlex
- W2885891351
- Cited by
- 377
- References
- 26
- Citations by year
- 2026: 43 · 2025: 77 · 2024: 60 · 2023: 63 · 2022: 51 · 2021: 43 · 2020: 30 · 2019: 9 · 2012: 1
- FWCI
- 7.29
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- BMC Biochemistry (publishedVersion, cc-by)
- Europe PMC (PubMed Central) (publishedVersion, other-oa)
- PubMed Central (publishedVersion, cc-by)
- PubMed (publishedVersion)
- DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Redox biology and oxidative stress
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Cancer and biochemical research
- Health Sciences › Medicine › Biochemistry › Antioxidant Activity and Oxidative Stress
- Keywords
- catalase activity, spectrophotometric assay, hydrogen peroxide decomposition, erythrocyte lysate, tissue homogenates, erythrocytes, liver tissue, kidney tissue, bacterial catalase
- MeSH terms
- Bacteria, Catalase, Cobalt, Erythrocytes, Humans, Hydrogen Peroxide, Kidney, Liver, Spectrophotometry, Ultraviolet, Reproducibility of Results, Artifacts, Enzyme Assays
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