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The removal of model viruses, poliovirus type 1 and canine parvovirus, during the purification of human albumin using ion-exchange chromatographic procedures.

The manufacturing process for albumin in Australia is based primarily on ion-exchange chromatography. The capacity of ion-exchange matrices to remove non-enveloped viruses (canine parvovirus and poliovirus type 1) was assessed using a scaled-down chromatographic process which was shown to yield product meeting purity criteria set for the manufacturing process. Poliovirus type 1 and canine parvovirus were added at one tenth the volume of desalted and delipidated Supernatant II + III produced by traditional Cohn Fractionation from human plasma before the material was applied to DEAE and CM ion-exchangers connected in series. Samples were taken at equilibration, wash, elution and regeneration steps and the log clearance and reduction of the viruses calculated. The mean clearance and reduction factors for viral load of poliovirus type 1 were 5.3 logs and 3.2 logs, respectively and 1.8 logs and 1.8 logs for canine parvovirus.