A heparin-binding domain of human von Willebrand factor. Characterization and localization to a tryptic fragment extending from amino acid residue Val-449 to Lys-728.
1987; Elsevier BV; Volume: 262; Issue: 4 Linguagem: Inglês
10.1016/s0021-9258(19)75700-7
ISSN1083-351X
AutoresYoshihiro Fujimura, Koiti Titani, Linda Z. Holland, James R. Roberts, Paul J. Kostel, Z M Ruggeri, T S Zimmerman,
Tópico(s)Platelet Disorders and Treatments
ResumoWe have recently shown that the domain of von Willebrand factor (vWF) which interacts with the platelet glycoprotein Ib (GPIb) is located in a 52/48-kDa tryptic fragment of the molecule which begins with amino acid residue Val-449.We have now established that the fragment extends to residue Lys-728 and demonstrate here that a high affinity heparinbinding domain of vWF also lies within this region and in close proximity to that for GPIb.We have used an assay employing heparin coupled to Sepharose CL-GB to show that "'I-vWF binds to heparin in a timedependent, saturable, and reversible manner.Binding could be completely inhibited by the 52/48-kDa fragment, but was not affected by other tryptic fragments of 55, 41, 13, and 22 kDa.NHz-terminal sequencing of these fragments showed that they were derived from different parts of the molecule, as follows: 13 kDa,
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