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Analytical ultracentrifugation of the factor VIII-Von Willebrand factor showed an apparently homogenous protein with an S° of 29. With the diffusion coefficient D of 1.24 x 10-7 cm2/ sec.(obtained by 20,w double diffusion of the protein and the immunochemically equivalent amount of rabbit anti-factor VIII) a mean mol. wt. of 2.2 x 106 and a friction ratio of 1.9 are derived. Turbidity measurements confirmed the high mol. wt. and resulted in an estimation of the co-volume of the protein. The free electric mobility wasfound to be 3.6 x 10-5 cm2/Vsec at pd 7.00 and 8.5x 10-5cm2/V sec at pH 8.80, while iso-electric focussing patterns of the native protein and the polypeptide (mol.wt. 260 000) obtained by reduction in the presence of urea exhibited a maximum at about pH 4.5. The apparent D found upon electrophoresis is an order higher than given above and is dependent on the field strength. The heterogeneity indicated by this phenomenon was confirmed by reversal electrophoresis (yielding a decrease in the apparent D). Since continuous immuno precipitation lines are found upon cross-electrophoresis, we interprete the results in terms of a series of closely related oligomers with a mean number of 8 polypeptidechains and a variation from about 6 to 10.

Physicochemical Characteristics of the Human Factor VIII-Von Willebrand Factor Oligomers