Studies on the Nature of Antihemophilic Factor (Factor VIII): FURTHER EVIDENCE RELATING THE AHF-LIKE ANTIGENS IN NORMAL AND HEMOPHILIC PLASMAS

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Abstract

Normal human antihemophilic factor (AHF, factor VIII) and the protein antigenically related to it in hemophilic plasma both appeared in the void volume of columns of agarose (Sepharose 4B) during purification of these agents. On ultracentrifugation upon sucrose gradients, both agents had sedimentation characteristics similar to those of an S30 marker. After reduction, the polypeptide chains of purified normal AHF and of the nonfunctional agent from hemophilic patients had an apparent molecular weight of 200,000 as determined by sodium dodecyl sulfate polyacrylamide gel electrophoresis. These observations suggest that AHF, purified as described, exists as a large molecule with subunits of molecular weight of approximately 200,000.

Authors

Bruce Bennett, Walter B. Forman, Oscar D. Ratnoff