The purification of antibodies is conventionally performed using affinity chromatography columns, with Protein A as ligand. The development of valid alternatives to Protein A is one of the challenges of the research in downstream processing, which becomes more important as the production capability of the biopharmaceutical industry increases. The objective of this work is the characterization of affinity membranes derivatized with two different synthetic ligands that show high specificity for immunoglobulins. The affinity membranes have been prepared and characterized, in view of their application in the capture purification step.

Development and Characterization of Affinity Membranes for Immunoglobulin Purification / Boi, Cristiana; Sarti, GIULIO CESARE. - In: SEPARATION SCIENCE AND TECHNOLOGY. - ISSN 0149-6395. - STAMPA. - 42:(2007), pp. 2987-3001. [10.1080/01496390701560140]

Development and Characterization of Affinity Membranes for Immunoglobulin Purification

BOI, CRISTIANA;SARTI, GIULIO CESARE
2007

Abstract

The purification of antibodies is conventionally performed using affinity chromatography columns, with Protein A as ligand. The development of valid alternatives to Protein A is one of the challenges of the research in downstream processing, which becomes more important as the production capability of the biopharmaceutical industry increases. The objective of this work is the characterization of affinity membranes derivatized with two different synthetic ligands that show high specificity for immunoglobulins. The affinity membranes have been prepared and characterized, in view of their application in the capture purification step.
2007
Development and Characterization of Affinity Membranes for Immunoglobulin Purification / Boi, Cristiana; Sarti, GIULIO CESARE. - In: SEPARATION SCIENCE AND TECHNOLOGY. - ISSN 0149-6395. - STAMPA. - 42:(2007), pp. 2987-3001. [10.1080/01496390701560140]
Boi, Cristiana; Sarti, GIULIO CESARE
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Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/11585/49989
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