Ion exchange chromatography was carried out using a HiTrap DEAE-sepharose fast Flow column (Amersham Pharmacia, Uppsala, Sweden) equilibrated with 10 mmol/l Tris–HCl buffer (pH 7.5) on the ÄKTA explorer 100 system obtained from Amersham Biosciences (Sweden). The proteins bound to the column were eluted sequentially using 0.05, 0.1, 0.2, 0.3, 0.45, 0.6, and 1.0 mol/l NaCl. The eluate was assessed via its absorbance at 280 nm. Each fraction was dialyzed and adjusted to the same concentration using Tris–HCl buffer. The antifungal activity of each fraction was tested against R. cerealis using the agar-diffusion method described above.
Hitrap deae sepharose fast flow column
Manufactured by Cytiva
Sourced in Sweden
The HiTrap DEAE-Sepharose Fast Flow column is a pre-packed chromatography column designed for the purification of biomolecules. It utilizes DEAE (Diethylaminoethyl) functional groups on a Sepharose matrix to enable ion exchange chromatography. The column is intended for fast flow separations and can be used with a variety of sample types and buffer conditions.
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Lab products found in correlation
3 protocols using hitrap deae sepharose fast flow column
1
Ion Exchange Chromatography of Antifungal Proteins
2
Ion Exchange Chromatography for Antifungal Purification
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Ion exchange chromatography was carried out using a HiTrap DEAE-sepharose fast Flow column (Amersham Pharmacia, Uppsala, Sweden) equilibrated with 10 mmol/l Tris-HCl buffer (pH 7.5) on the ÄKTA explorer 100 system obtained from Amersham Biosciences (Sweden). The proteins bound to the column were eluted sequentially using 0.05, 0.1, 0.2, 0.3, 0.45, 0.6, and 1.0 mol/l NaCl. The eluate was assessed via its absorbance at 280 nm. Each fraction was dialyzed and adjusted to the same concentration using Tris-HCl buffer. The antifungal activity of each fraction was tested against R. cerealis using the agar-diffusion method described above.
3
Ion Exchange Chromatography Separation
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Ion exchange chromatography was carried out using a HiTrap DEAE-sepharose fast Flow column (Amersham Pharmacia, Sweden) equilibrated with 10 mmol/l Tris-HCl buffer (pH 7.5) on the ÄKTA explorer 100 system obtained from Amersham Biosciences (Sweden). The proteins bound to the column were eluted sequentially using 0.05, 0.1, 0.2, 0.3, 0.45, 0.6, and 1.0 mol/l NaCl. The eluate was assessed via its absorbance at 280 nm. Each fraction was dialyzed and adjusted to the same concentration using Tris-HCl buffer. The antifungal activity of each fraction was tested against R. cerealis using the agardiffusion method.
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