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Isolation and characterization of a collagen binding domain in human von Willebrand factor.

von Willebrand factor binds to fibrillar type I collagen in a rapid, temperature-independent, reversible, specific, and saturable manner. Evaluation of binding isotherms by Scatchard-type analysis demonstrated that 6-18 micrograms of von Willebrand factor bind per mg of collagen, with Ka between 2 and 8 X 10(8) M-1. Five distinct tryptic fragments, purified under denaturing and reducing conditions and representing over 75% of the molecular mass of the von Willebrand factor subunit, were tested for their capacity to inhibit the von Willebrand factor-collagen interaction. Complete inhibition was obtained with a 52/48-kDa fragment at a concentration of approximately 1 microM. The location of this fragment in the subunit was established to be between Val-449 and Lys-728. Fifteen monoclonal antibodies against the 52/48-kDa fragment inhibited von Willebrand factor binding to collagen. Six antibodies against other portions of the von Willebrand factor subunit had no inhibitory effect. The tryptic fragment was a competitive inhibitor of von Willebrand factor binding to collagen and, therefore, recognizes the same interaction site as the intact molecule. These studies precisely define a domain in the von Willebrand factor subunit that interacts with type I collagen.

Pubmed ID: 3490481

Authors

  • Pareti FI
  • Fujimura Y
  • Dent JA
  • Holland LZ
  • Zimmerman TS
  • Ruggeri ZM

Journal

The Journal of biological chemistry

Publication Data

November 15, 1986

Associated Grants

  • Agency: NHLBI NIH HHS, Id: HL 15491
  • Agency: NHLBI NIH HHS, Id: HL 31950
  • Agency: NCRR NIH HHS, Id: RR 00833

Mesh Terms

  • Antibodies, Monoclonal
  • Antigen-Antibody Complex
  • Binding Sites
  • Collagen
  • Humans
  • Kinetics
  • Peptide Fragments
  • Protein Binding
  • Thermodynamics
  • Trypsin
  • von Willebrand Factor