Abstract:
Methods for the preparation of concentrates of factor VIII, factor IX, high purity factor IX, Cl esterase inhibitor, specific immunoglobulin and platelet factor XIII are described. These procedures were developed or modified with the aim of integration into an automated process that would allow sequential recovery of all the clinically significant trace proteins from a single plasma pool. Concomitant recovery of important proteins such as transferrin, alpha-1-antitrypsin and platelet-derived growth factor was considered.
A high-purity factor VIII concentrate heat-treated at 80°C for 96 h was prepared by a process that incorporated heparin fractionation. This method was shown to be suitable for assimilation into an existing regional blood processing laboratory. Several ion-exchange procedures for the recovery of factor IX were evaluated and higher purification of a factor IX concentrate was achieved on a new cellulose-based chromatographic medium. A chromatographic procedure for the preparation of a heat-treated high-purity Cl esterase inhibitor concentrate was described and the performance of a new cellulose-based desalting medium was evaluated in comparison with ultrafiltration. A heat-treated specific immunoglobulin concentrate was prepared from side-stream fractions of an automated chromatographic process for the production of albumin concentrate, and a pilot study for the fractionation of outdated platelet concentrates was carried out with the aim preparing components of potential therapeutic value. See summary flow diagrams of fractionation processes included with references in the back of this thesis.
