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The nature of sugar chain of factor VIII related protein (VIIIR) in the plasma of normal subject and patients with type I and IIA of von Willebrands disease was examined by crossed affinoimmunoelectrophoresis using anti-human factor VIII rabbit serum, with inserted wheat germ agglutinin (WGA) agarose layer. Molecular weight disf ribution and affinity for WGA of factor VIII related antigen (VIIIR: AG) were estimated by the electrophoretic patterns. VIIIR: AG, in normal plasma and in type I of von Willebrands disease, showed high affinity for WGA at the portion over 3X106 daltons of molecular weight. On the other hand, VIIIR: AG in plasma of type IIA consists only of the multimers smaller than 3 X 106 daltons, showing a very weak affinity for WGA. These results suggested that VIIIR-multimers in type IIA may be poor in sialic acid reactive with WGA, in addition to incomplete polymerization.

Factor VIII related protein in von Willebrand's disease Analysis by crossed affinoimmunoelectrophoresis using wheat germ agglutinin