Removal of sodium dodecyl sulphate from proteins by gel permeation chromatography
β Scribed by Batia Kaplan; Mordechai Pras
- Book ID
- 107996621
- Publisher
- Elsevier Science
- Year
- 1987
- Weight
- 216 KB
- Volume
- 423
- Category
- Article
- ISSN
- 0378-4347
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π SIMILAR VOLUMES
Effective removal of sodium dodecyl sulfate from proteins in water or sodium phosphate buffer was achieved by column chromatography using the ion-retardation resin AG11A8. An average recovery of 83% protein was obtained, while 0.1 to 1.4 moles of sodium dodecyl sulfate remained on each mole of prote
The inclusion of urea has been found to eliminate adsorption of proteinsodium dodecyl sulphate (SDS) complexes to controlled pore glass. Using buffer containing 6 M urea, 0.5 "A, SDS and glass with pore diameter 12.3 nm, it is possible to determine protein molecular weights in the range 3500-12,000.
The ability of two high-performance liquid chromatography gel permeation columns to separate proteins was evaluated. These columns gave satisfactory molecular weight separations for some, but not all, proteins tested. These results indicate that there are limitations in confidence of molecular weigh