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The relation between the VWF-A of F VIII-VWF and its multimeric structure was studied in an annular perfusion chamber according to Baumgartner, with a steady flow system.  51Cr-labelled aspirin treated human platelets and human post mortem renal arteries were employed. F VIII-VWF was purified from cryoprecipitate by agarose gel chromatography and radiolabelled by the lactoperoxydase method. The multimeric distribution was determined by SDS-agarose electrophoresis. Five different commercial high purity concentrates contained multimers between 0.5 and 3.5 x 106 mol wt. None of these concentrates had VWF-A at ristocetin cofactor activities (RIC0F-A) of 1.0 u/ml. A low potency concentrate with mul- timers in the same mol wt range had normal VWF-A. Mild reduction (dithioerythritol-DTE ≤ 2mM) caused a shift in , mol wt range from 3.0 - 20.0 × 106 towards 0.5 - 2.0 × 106 with little decrease in RIC0F-A and VWF-A. Reduction with 10 mM DTE produced multimers of 1.5 and 0.5 × 106 without RICOF-A and VWF-A, but binding normally to the vessel wall. The void volume peak of 125I-VIII-VWF was rechromatographed on Sepharose-2B and arbitrarily divided in fractions A: mol wt 8,0 - 18.0 × 106 ;B: mol wt 4.5 - 11.0 × 106 ; and C: mol wt 2.5 - 6.5 × 106 . Binding of 125I-VIII-VWF to the subendothelium was highest for A, intermediate for B and lowest for C. Correction for mean mol wt showed that almost equal numbers of molecules bound from all three fractions. When the quantity of bound VIII-VWF was thus expressed, all fractions had a similar relative VWF-A.  These data indicate that high purity concentrates do not correct the bleeding time at normal RICOF-levels, because they lack VWF-A. Multimers of high mol wt normally carry both RICOF-A and VWF-A, but the high mol wt is no absolute requirement. These data are in agreement with the notion that VWF-A resides on a specific polypeptide chain in the molecule.

thrombosis and haemostasis

The Relationship Between The Multimeric Structure Of F VIII-VWF And The Facilitation Of Platelet Adhesion To Human Subendothelium (Von Willebrand Factor Activity VWF-A)