Preprint Article Version 1 This version is not peer-reviewed

New Spectrophotometric Method for the Assessment of Catalase Enzyme Activity in Biological Tissues

Version 1 : Received: 26 October 2019 / Approved: 29 October 2019 / Online: 29 October 2019 (04:04:50 CET)

A peer-reviewed article of this Preprint also exists.

Thulfeqar A. Hamza and Mahmoud H. Hadwan*, “New Spectrophotometric Method for the Assessment of Catalase Enzyme Activity in Biological Tissues”, Current Analytical Chemistry (2020) 16: 1. https://doi.org/10.2174/1573411016666200116091238 Thulfeqar A. Hamza and Mahmoud H. Hadwan*, “New Spectrophotometric Method for the Assessment of Catalase Enzyme Activity in Biological Tissues”, Current Analytical Chemistry (2020) 16: 1. https://doi.org/10.2174/1573411016666200116091238

Journal reference: Current Analytical Chemistry 2020, 16
DOI: 10.2174/1573411016666200116091238

Abstract

Background: Catalase is a vital antioxidant enzyme that dismutates H2O2 into water and molecular oxygen. Many protocols have been developed to measure catalase enzyme activity. Spectrophotometric methods are the most common assays that used to assess catalase enzyme activity. Methods: Because the rate-limiting step during catalase enzyme activity depends upon the dissociation of hydrogen peroxide, the developed assay measures the reaction between a hydroquinone/anilinium sulfate/ammonium molybdate reagent and Unreacted Hydrogen Peroxide, which results in the production of a purple, disubstituted quinone compound with a maximum absorbance value at 550 nm. Results: To clarify the precision of the developed method, the coefficients of variation were determined to be 2.6% and 4.7% for within run measurements and between run measurements, respectively. This method returned results that correlated well (r = 0.9982) with the results returned using the peroxovanadate method to assess catalase enzyme activity. Additionally, we examined the use of the newly developed hydroquinone assay to measure catalase enzyme activity in liver and bacterial homogenate samples. Conclusion: These results demonstrated that this assay can be used for scientific research and routine health applications because it is inexpensive, simple, accurate, and rapid. This method is suitable for use in clinical pathology laboratories because it is simple and produces precise and reproducible results.

Subject Areas

catalase activity; hydrogen peroxide; hydroquinone; anilinium sulfate; ammonium molybdate

Comments (0)

We encourage comments and feedback from a broad range of readers. See criteria for comments and our diversity statement.

Leave a public comment
Send a private comment to the author(s)
Views 0
Downloads 0
Comments 0
Metrics 0


×
Alerts
Notify me about updates to this article or when a peer-reviewed version is published.