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Revised Manuscript Received May 26, 1989 abstract: A 39/34-kilodalton (kDa) monomeric dispase fragment of von Willebrand factor (vWF) has been purified by heparin affinity chromatography. Detailed structural analysis of the individual 39-and 34-kDa fragments indicated that they had identical amino acid sequences extending from Leu-480/Val-481 to Gly-718with an intramolecular disulfide bond between Cys-509 and Cys-695. In addition to the binding site for heparin, the 39/34-kDa fragment also containedbinding sites for collagen and for platelet membrane glycoprotein (GP) lb. Unlike native vWF, the 39/34-kDa fragment bound to GP lb without the requirement for a modulator but showed increased binding in the presence of botrocetin. The 39/34-kDavWF fragment was cross-linked to intact human platelets by using the membrane-impermeable, homobifunctional cross-linking reagent bis (sulfosuccinimidyl …