Blood factor VIII purification

Many small proteins, in particular those that function extracellularly (e.g. insulin, GH and various cytokines) are quite stable and may be fractionated on a variety of HPLC columns without significant denaturation or decrease in bioactivity. Preparative HPLC is used in industrial-scale purification of insulin and of IL2. In contrast, many larger proteins (e.g. blood factor VIII) are relatively labile, and loss of activity due to protein denaturation may be observed upon high-pressure fractionation. 

Owing to the frequency of product administration, the purification procedure for recombinant factor VIII C must be particularly stringent. Unlike the situation pertaining when the product is purified from human blood, any contaminant present in the final product will be non-human and, hence, immunogenic. Sources of such contaminants would include ... 

The need to transfuse blood components such as plasma, platelets, factor VIII, in addition to red blood cells (RBC) has generated the development of plasmapheresis (plasma separation from whole blood) and more generally that of apheresis (fractionation of blood components). Plasma collection from donors by centrifugation of blood bags began only in 1944. This technique was extended to therapeutic plasma purification in 1950, but RBCs were fragilized by the centrifugation and the plasma was not completely platelet-free. 

Purification of a high molecular weight glycoprotein from human blood platelets Isolation of Factor VIII from human plasma Purification of human and rat plasma fibro-nectin... 

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