Identification of factor-XIIIa-reactive glutaminyl residues in the propolypeptide of bovine von Willebrand factor

J. Takagi, T. Aoyama, Shoko Ueki, H. Ohba, Y. Saito

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Von Willebrand factor is a large multimeric plasma protein which plays important roles in platelet aggregation, blood coagulation and probably also in the adhesion of endothelial cells. A 100-kDa propeptide, called the propolypeptide of von Willebrand factor (pp-vWF), is generated during biosynthesis. We found that pp-vWF served as a substrate for transglutaminases including human factor XIIIa and guinea pig liver transglutaminase [Usui, T., Takagi, J. and Saito, Y. (1993) J. Biol. Chem. 265, 12311-12316]. As such, it could form cross-linked copolymers with the extracellular matrix protein, laminin, making it all the more likely that pp-vWF plays a role in cell adhesion phenomena [Takagi, J., Sudo, Y., Saito, T. and Saito, Y. (1994) Eur: J. Biochem. 222, 861-867]. In this work, we identified the Gln residues in pp-vWF specifically reacting with blood coagulation factor XIIIa as amine accepters. The fluorescent amine, dansylcadaverine, was employed for labeling the enzyme-reactive sites of the protein. Following partial proteolysis, fragments containing the labeled Gln residues were isolated by passage through an anti-dansyl affinity chromatographic column. Amino acid sequence analyses of the fragments revealed that, out of about 40 Gln residues in pp-vWF, only four could be modified in the factor-XIIIa-catalyzed reaction.

Original languageEnglish
Pages (from-to)773-777
Number of pages5
JournalEuropean Journal of Biochemistry
Issue number3
Publication statusPublished - 1995
Externally publishedYes



  • Dansylcadaverine
  • Factor XIIIa
  • Propolypeptide
  • Transglutaminase
  • Von Willebrand factor

ASJC Scopus subject areas

  • Biochemistry

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