Separation of MBP fusion proteins through affinity membranes.
Cellulose microporous membranes have been modified in order to obtain a stationary phase specific for the recovery of a class of fusion proteins containing the maltose binding protein domain, through affinity chromatography separations. The feasibility of a single step separation process for the recovery of large amounts of the desired product has been considered. To that purpose, a preparative scale module has been realized, suitable for flat sheet membranes. The affinity matrix used proved to be highly selective toward the fusion proteins examined. The binding capacity determined is comparable with the nominal binding capacity of commercially available supports. The influence of the relevant working parameters, such as flow rate, on the performances of the recovery process has been studied.
Cattoli
Francesca
F
Dipartamento di Ingegneria Chimica, Mineraria e delle Tecnologie Ambientali, Università di Bologna, Viale Risorgimento 2, 40136 Bologna, Italy.
Sarti
Giulio C
GC
D001426:Bacterial Proteins / Q000302:isolation & purification / Q000493:pharmacokinetics; D002352:Carrier Proteins / Q000302:isolation & purification* / Q000493:pharmacokinetics; D002482:Cellulose; D002846:Chromatography, Affinity / Q000379:methods / Q000592:standards; D005240:Feasibility Studies; D058619:Maltose-Binding Proteins; D008567:Membranes, Artificial; D011993:Recombinant Fusion Proteins / Q000302:isolation & purification* / Q000493:pharmacokinetics
D001426:Bacterial Proteins; D002352:Carrier Proteins; D058619:Maltose-Binding Proteins; D008567:Membranes, Artificial; D011993:Recombinant Fusion Proteins; D002482:Cellulose