ArticleACS omega2026
A Convenient and Economical Spectrophotometric Assay for Ornithine Decarboxylase and Related Amino Acid Decarboxylases Using Sodium 2,4-Dinitrobenzenesulfonate.
Article in ACS omega, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
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4 authors.
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Abstract
Ornithine decarboxylase (ODC) catalyzes the conversion of l-ornithine into putrescine as the first and rate-limiting step in polyamine biosynthesis. Common assays used to measure ODC activity are often costly, involve expensive reagents and instruments, and require labor-intensive protocols. To address these issues, this research developed an economical and user-friendly spectrophotometric assay for ODC and other decarboxylases. The principle of the assay relies on the reaction of the ODC product, putrescine, with sodium 2,4-dinitrobenzenesulfonate (DNBS) under alkaline conditions, with heating at 70 °C for 1 h, generating a bis-2,4-dinitrophenyl derivative that is extracted in toluene and measured spectrophotometrically at 340 nm, providing a sensitive readout of enzyme activity. This assay demonstrates decent sensitivity, with a limit of detection (LOD) for inducible ODC activity as low as 0.21 μg/mL (5.1 pmol), and kinetic analysis revealed a
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