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  • Enhanced stability and decolorization of Coomassie Brilliant Blue R-250 by dextran aldehyde-modified horseradish peroxidase.

Enhanced stability and decolorization of Coomassie Brilliant Blue R-250 by dextran aldehyde-modified horseradish peroxidase.

Artificial cells, blood substitutes, and immobilization biotechnology (2010-12-02)
Melda Altikatoglu, Mithat Celebi
摘要

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.

材料
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产品描述

Sigma-Aldrich
酸性蓝83, 250, for microscopy
Sigma-Aldrich
酸性蓝83, pure
Sigma-Aldrich
酸性蓝83, Dye content ~50 %, Technical grade
Sigma-Aldrich
亮蓝R染色液, suitable for (for immunoelectrophoresis protein staining)
Sigma-Aldrich
亮蓝R浓缩液, suitable for SDS-PAGE, methanol solution