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Cited by 377Redox biology and oxidative stressCancer and biochemical researchAntioxidant Activity and Oxidative Stress

The DOI matches its Crossref record; 26 of the 26 references it cites were found in a registry or an index.

Simple spectrophotometric assay for measuring catalase activity in biological tissues

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Hadwan, Mahmoud Hussein·2018·BMC Biochemistry
DOI 10.1186/s12858-018-0097-5PMC PMC6091033
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Abstract

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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Crossref · 10.1186/s12858-018-0097-5

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Figures

Fig. 1 The spectrophotometric properties of the carbonato-cobaltate(III) complex that correlates with the activity of catalase enzyme. a A carbonato-cobaltate(III) complex. b Decreased color intensity in association with increased catalase activity. c Absorption spectra obtained for the colorimetric products of the present assay
Fig. 1 The spectrophotometric properties of the carbonato-cobaltate(III) complex that correlates with the activity of catalase enzyme. a A carbonato-cobaltate(III) complex. b Decreased color intensity in association with increased catalase activity. c Absorption spectra obtained for the colorimetric products of the present assayCC BY · PubMed Central
Fig. 2 The absorbance of carbonato-cobaltate(III) complex ([Co(CO3)3]Co) as a function of the incubation time of H2O2 alone (●) or H2O2 mixed with catalase enzyme (0.86 U mL−1) (▲)
Fig. 2 The absorbance of carbonato-cobaltate(III) complex ([Co(CO3)3]Co) as a function of the incubation time of H2O2 alone (●) or H2O2 mixed with catalase enzyme (0.86 U mL−1) (▲)CC BY · PubMed Central
Fig. 3 The catalase activities measured by the carbonato-cobaltate(III) complex method versus those expected for red blood cell homogenate at different dilutions
Fig. 3 The catalase activities measured by the carbonato-cobaltate(III) complex method versus those expected for red blood cell homogenate at different dilutionsCC BY · PubMed Central
Fig. 4 The catalase activity of liver and kidney tissues homogenates measured with the carbonato-cobaltate(III) complex method in comparison to that with the dichromate method
Fig. 4 The catalase activity of liver and kidney tissues homogenates measured with the carbonato-cobaltate(III) complex method in comparison to that with the dichromate methodCC BY · PubMed Central
Fig. 5 The catalase activity of Escherichia coli and Staphylococcus aureus measured with the carbonato-cobaltate(III) complex method in comparison to that with the Iwase et al. [26]
Fig. 5 The catalase activity of Escherichia coli and Staphylococcus aureus measured with the carbonato-cobaltate(III) complex method in comparison to that with the Iwase et al. [26]CC BY · PubMed Central

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Research works printed but not linked: 2

  1. Euler HV, Josephson K. Über katalase. I European J Org Chem. 1927;452:158–81.
  2. Masschelein W, Denis M, Ledent R. Spectrophotometric determination of residual hydrogen peroxide. Water Sewage Works. 1977;8:69–72.

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Metadata

Authors
Hadwan, M. H.
Affiliations
University of Babylon (IQ)
Corresponding author
Hadwan, Mahmoud Hussein
ORCID
Hadwan, Mahmoud Hussein
Venue
BMC Biochemistry
Publisher
Springer Science and Business Media LLC
Published
2018-08-03
Volume
19
Issue
1
Pages
7-7
ISSN
1471-2091 (ISSN-L)
DOI
10.1186/s12858-018-0097-5
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
FWCI
7.29
Type
journal article
Language
en
Open access
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 (medical) › 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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