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Hemoglobin depletion from red blood cell cytosol reveals new proteins in 2-D gel-based proteomics study
Dipankar Bhattacharya1, Debashis Mukhopadhyay, Abhijit Chakrabarti
1Biophysics Division, Saha Institute of Nuclear Physics, Kolkata, India.
Proteomics studies to identify proteins in the erythrocyte cytosol have been largely affected by the huge abundance of hemoglobin (Hb), which masks the detection of other proteins in the 2-D gel-based separation. We have depleted Hb effectively from erythrocyte cytosol using cation exchange chromatography and have detected more than 600 protein spots in the Hb depleted hemolysate using 2-DE. We have so far identified 59 proteins in the Hb-depleted cytosol of normal erythrocytes, including 10 proteins not identified before.
Proteomics studies to identify proteins in the erythrocyte cytosol have been largely affected by the huge abundance of hemoglobin (Hb), which masks the detection of other proteins in the 2-D gel-based separation. We have depleted Hb effectively from erythrocyte cytosol using cation exchange chromatography and have detected more than 600 protein spots in the Hb depleted hemolysate using 2-DE. We have so far identified 59 proteins in the Hb-depleted cytosol of normal erythrocytes, including 10 proteins not identified before.
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