Improved visualisation of high-molecular-weight von Willebrand factor multimers

• References

• 1 Tsai HM. Physiologic cleavage of von Willebrand factor by a plasma protease is dependent on its conformation and requires calcium ion. Blood 1996; 87: 4235-4244.
• 2 Furlan M, Robles R, Lämmle B. Partial purification and characterization of a protease from human plasma cleaving von Willebrand factor to fragments produced by in vivo proteolysis. Blood 1996; 87: 4223-4.
• 3 Budde U. Phenotypic classification of von Willebrand disease. Haematologica Reports 2005; 1: 9-15.
• 4 Raines G, Aumann H, Sykes S. et al Multimeric analysis of von Willebrand factor by molecular sieving electrophoresis in sodium dodecyl sulphate agarose gels. Thromb Res 1990; 60: 201-212.
• 5 Furlan M, Robles R, Affolter D. et al Triplet structure of von Willebrand factor reflects proteolytic degr degradation of high molecular weight multimers. Proc Natl Acad Sci USA 1993; 90: 7503-7507.
• 6 Dent JA, Berkowitz SD, Ware J. et al Identification of a cleavage site directing the immunochemical detection of molecular abnormalities in type IIAh von Willebrand factor. Proc Natl Acad Sci USA 1990; 87: 6306-6.