Response to commercial factor VIII concentrate

Molecular characterization of commercial porcine factor VIII concentrate.

Commercial porcine factor VIII concentrate (Hyate:C) is effective in treatment of patients with hemophilia A who have circulating antibodies to factor VIII. The molecular forms of factor VIII in the concentrate were identified and evaluated in light of the known properties of porcine and human factor VIII. The factor VIII in the concentrate was isolated by tandem chromatography on gelatin-Sepha...

Isolation and characterization of human factor VIII: molecular forms in commercial factor VIII concentrate, cryoprecipitate, and plasma.

Human factor VIII has been isolated from a high purity factor VIII concentrate by immunoaffinity chromatography and HPLC on Mono Q gel. Two fractions of factor VIII were obtained with a specific activity of approximately equal to 7000 units/mg. The major fraction contained eight peptide chains of 200, 180, 160, 150, 135, 130, 115, and 105 kDa plus one doublet chain of 80 kDa. The minor fraction...

Small Pool Heat-treated Intermediate Purity Factor Viii Concentrate

Antibodies to factor VIII. V. Patterns of immune response to factor VIII in hemophilia A.

The natural history of factor VIII antibodies was studied in 20 severe, multitransfused hemophiliacs. Two patterns of humoral immune reactivity were observed. In one group of ten, who developed antibodies after an average of 22 cumulative exposure days to factor VIII, the antibody titers increased after each antigenic stimulation or persisted for years in the absence of transfusion. These patie...

Comparison of factor VIII-related von Willebrand factor proteins prepared from human cryoprecipitate and factor VIII concentrate.

Both commercial factor VIII concentrate and cryoprecipitate have factor VIII coagulant activity and factor VIII antigen (VIIIR:Ag). but the concentrate lacks the von Willebrand activity (VIIIR:WF) found in the cryoprecipitate. In an effort to find a possible cause for this anomaly we compared the structures of VlllR:WF proteins responsible for the VllIR:Ag and VlllR:WF activities obtained from ...