Separation of proteins using hydrophobic interaction membrane chromatography
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Membrane chromatography can overcome some of the problems associated with packed bed chromatography. In most membrane chromatographic studies reported so far, ion-exchange and affinity interactions have been utilised. In this paper the use of hydrophobic interactions for chromatographic separation is described. A polyvinylidene fluoride membrane was identified which could bind specific proteins in the presence of high ammonium sulphate concentration. The separation of CAMPATH-IG monoclonal antibody and bovine serum albumin using this membrane is discussed.
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