Properties of a new intravenous immunoglobulin (IGIV-C, 10%) produced by virus inactivation with caprylate and column chromatography.

Background And Objectives: Current manufacture of intravenous immunoglobulin (Gamimune N) uses four cold-ethanol precipitation steps and solvent-detergent treatment. Our objective was to design a new manufacturing process to maximize immunoglobulin G (IgG) purity, achieve robust viral safety, preserve all the biological activities of antibody and avoid unnecessary protein loss.

Materials And Methods: The new process combines multiple functions in single steps.

Evaluation of virus and prion reduction in a new intravenous immunoglobulin manufacturing process.

Background And Objectives: Minimizing the transmission risk of infectious diseases is of primary importance in the manufacture of products derived from human plasma. A novel chromatography-based intravenous immunoglobulin (IGIV) manufacturing process was developed and the reduction of virus and transmissible spongiform encephalopathies (TSE) during the manufacturing process was assessed. Mechanistically distinct steps that could affect virus reduction were identified, and the robustness of virus reduction over the range of process conditions was determined.

Enveloped virus inactivation by caprylate: a robust alternative to solvent-detergent treatment in plasma derived intermediates.

Solvent-detergent treatment, although used routinely in plasma product processing to inactivate enveloped viruses, substantially reduces product yield from the human plasma resource. To improve yields in plasma product manufacturing, a new viral reduction process has been developed using the fatty acid caprylate. As licensure of plasma products warrants thorough evaluation of pathogen reduction capabilities, the present study examined susceptibility of enveloped viruses to inactivation by caprylate in protein solutions with varied pH and temperature.

Purification of alpha 1 proteinase inhibitor from human plasma fraction IV-1 by ion exchange chromatography.

Background And Objectives: Alpha-proteinase inhibitor (PI) protects the lungs from proteolytic damage caused by elastase and can be used to treat congenital emphysema. We describe an improved method of purification of alpha 1 PI from redissolved fraction IV-1 paste.

Materials And Methods: The process used dimethylaminoethyl anion exchange chromatography, sulfopropyl cation exchange chromatography, virus inactivation by dry heat, and tri-n-butyl-phosphate/cholate treatment, followed by a second strong cation exchange chromatography.

Chromatographic purification of human alpha 1 proteinase inhibitor from dissolved Cohn fraction IV-1 paste.

A novel chromatographic process for purification of alpha 1 proteinase inhibitor (alpha 1-PI) from Cohn fraction IV-1 paste is described. This process has been successfully scaled up to 50-1 columns. It involves DEAE chromatography, sulfopropyl (S) cation chromatography, tri-n-butyl phosphate (TNBP)-cholate treatment, a second S cation chromatography, freeze-drying and dry-heat.