## Abstract Protein elution curves in ion exchange chromatography (IEC) were simulated with a rate model. Three pure proteins and their mixture were used (Ξ±βlactalbumin, BSA, and conalbumin) under different operational conditions. The anionic matrix QβSepharose FF was used packed in a 1βmL column.
Protein separation by ion exchange chromatography: A model for gradient elution
β Scribed by K. Kang; B. J. McCoy
- Publisher
- John Wiley and Sons
- Year
- 1989
- Tongue
- English
- Weight
- 397 KB
- Volume
- 33
- Category
- Article
- ISSN
- 0006-3592
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Elution curves in ionic exchange chromatography (IEC) for a three-protein mixture (alpha-lactoalbumin, ovalbumin, and beta-lactoglobulin), carried out under different flow rates and ionic strength conditions, were simulated using two different mathematical models. These models were the Plate Model a
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