ArticlePloS one2013
A highly sensitive method for quantitative determination of L-amino acid oxidase activity based on the visualization of ferric-xylenol orange formation.
Article in PloS one, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.
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Who cites it
4 citing papers in PubMed, 18 citations in OpenAlex.
- A Xylenol Orange-Based Screening Assay for the Substrate Specificity of Flavin-Dependent para-Phenol Oxidases.Molecules (Basel, Switzerland) · 2018Article
- Oxidative Stress Induced by Polymyxin E Is Involved in Rapid Killing ofBioMed research international · 2017Article
- Focused Directed Evolution of Aryl-Alcohol Oxidase in Saccharomyces cerevisiae by Using Chimeric Signal Peptides.Applied and environmental microbiology · 2015Article
- Exploring regulation genes involved in the expression of L-amino acid oxidase in Pseudoalteromonas sp. Rf-1.PloS one · 2015Article
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
L-amino acid oxidase (LAAO) has important biological roles in many organisms, thus attracting great attention from researchers to establish its detection methods. In this study, a new quantitative in-gel determination of LAAO activity based on ferric-xylenol orange (Fe(III)XO) formation was established. This method showed that due to the conversion of Fe(II) to Fe(III) by H2O2 and subsequent formation of Fe(III)XO complex halo in agar medium, the logarithm of H2O2 concentration from 5 to 160 µM was linearly correlated to the diameter of purplish red Fe(III)XO halo. By extracting the LAAO-generated H2O2 concentration, the LAAO activity can be quantitatively determined. This Fe(III)XO agar assay is highly sensitive to detect H2O2 down to micromolar range. More importantly, it is easy to handle, cheap, reproducible, convenient and accurate. Coupled with SDS-PAGE, it can directly be used to determine the number and approximate molecular weight of LAAO in one assay. All these features make this in-gel Fe(III)XO assay useful and convenient as a general procedure for following enzyme purification, assaying fractions from a column, or observing changes in activity resulting from enzyme modifications, hence endowing this method with broad applications.
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