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Updated: Jun 6, 2026

Staining of Proteins in Gels with Coomassie G-250 without Organic Solvent and Acetic Acid
Published on: August 14, 2009
Enhanced stability and decolorization of Coomassie Brilliant Blue R-250 by dextran aldehyde-modified horseradish
Melda Altikatoglu1, Mithat Celebi
1Yildiz Technical University, Faculty of Arts and Sciences, Department of Chemistry, Istanbul, Turkey. maltikatoglu@yahoo.com
Abstract:
Horseradish peroxidase (EC 1.11.1.7) was chemically modified by periodate-activated dextran. The activities of free and modified enzyme against organic-aqueous interface and some chemicals were determined. Modified HRP remained fully active in the presence of organic solvent for 4 h. However, the unmodified enzyme lost 50% of its activity within the first 2 h. The effects of possible inhibitors on enzyme activity were investigated. In addition, Coomassie Brilliant Blue R-250 was efficiently decolorized using the free and modified HRP. After 5 minutes of treatment, the color removal of dye was 80-90%. Modified HRP showed effective performance compared to free HRP.
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