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Separation of proteins using hydrophobic interaction membrane chromatography
1Department of Engineering Science, University of Oxford, UK. raja.ghosh@eng.ox.ac.uk
Journal of Chromatography. A
|August 21, 2001
Summary
Hydrophobic interaction membrane chromatography offers an alternative to traditional methods. This study demonstrates its use for separating specific proteins like CAMPATH-IG monoclonal antibody.
Area of Science:
- Biochemistry
- Biotechnology
- Separation Science
Background:
- Packed bed chromatography faces limitations in certain applications.
- Existing membrane chromatography often relies on ion-exchange or affinity interactions.
- Hydrophobic interaction chromatography (HIC) is a valuable separation technique.
Purpose of the Study:
- To explore the application of hydrophobic interactions in membrane chromatography.
- To identify a suitable membrane for hydrophobic protein binding.
- To demonstrate the separation of specific proteins using this novel approach.
Main Methods:
- Utilized a polyvinylidene fluoride (PVDF) membrane.
- Employed high ammonium sulphate concentrations to induce hydrophobic binding.
- Applied membrane chromatography for protein separation.
Main Results:
- Identified a PVDF membrane capable of binding specific proteins under high salt conditions.
- Successfully separated CAMPATH-IG monoclonal antibody and bovine serum albumin.
- Demonstrated the efficacy of hydrophobic interaction membrane chromatography.
Conclusions:
- Hydrophobic interaction membrane chromatography is a viable technique.
- PVDF membranes can be effectively used for HIC.
- This method offers a promising alternative for protein purification.