STUDY ON THE FUNCTIONAL DOMAINS OF VON WILLEBRAND FACTOR IN PATIENTS WITH VON WILLEBRAND DISEASE

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The functional domains of von Willebrand favtor (vWf)(1) The amino-terminal fragment of vWf (III-T4), which includes factor VIII-binding domain, was purified from the trypsin-digestions of vWf. Five monoclonal antibodies (MAbs) agaist to vWf were produced and were determined the epitopes on vWf. Epitopes of four MAbs (464,418,511,522) were located in III-T4, one (516) did not recognized on III-T4. Four MAbs (464,418,522,516) inhibited the binding of factor VIII to vWf. MAb (418) recognized on the conformational structure of vWf. On the other hand, MAb (522) detected on the linear structure of vWf. Now, we analyze further closed epitopes of these MAbs.(2) We found a patient with plasma vWf which was not reacted with MAb (522). We are going to study further investigation of this plasma vWF.2. The analysis of plasma vWf in patients with various types of von willebrand disease (vWd)(1) We established the method of the analysis for reduced vWf using a minute amount of plasma without purification.(2) We analyzed reduced plasma vWf in patients with various types of vWd and discoverd two patients with abnormal proteolytic reduced fragment in type I vWd.(3) These patients with abnormal reduced fragment in type I vWd have a point mutaion, Arg611 to His.(4) We have now researched the family members of these patients with abnormal reduced plasma vWf and was assayd the functional activities of plasma vWf.