Separation of proteins using hydrophobic interaction membrane chromatography.
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.
Ghosh
R
R
Department of Engineering Science, University of Oxford, UK. raja.ghosh@eng.ox.ac.uk
D000818:Animals; D000911:Antibodies, Monoclonal; D002417:Cattle; D002845:Chromatography / Q000379:methods*; D008567:Membranes, Artificial; D011145:Polyvinyls; D011506:Proteins / Q000302:isolation & purification*; D012710:Serum Albumin, Bovine / Q000302:isolation & purification; D005465:Fluorocarbon Polymers
D000911:Antibodies, Monoclonal; D008567:Membranes, Artificial; D011145:Polyvinyls; D011506:Proteins; D012710:Serum Albumin, Bovine; C024865:polyvinylidene fluoride; D005465:Fluorocarbon Polymers