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An anti-EGF monoclonal antibody that detects intramolecular communication in factor IX

In English

Författare

Summary, in English

Coagulation factor IX contains a gamma-carboxyglutamic acid (Gla) module, two epidermal growth factor-like (EGF) modules, and a serine protease region. We have characterized a mouse monoclonal antibody that binds the N-terminal EGF-like module of human factor IX with high affinity. Studies of recombinant factor IX mutants indicated that the epitope is located in the C-terminal end of the EGF-like module, which is consistent with the binding being non-Ca(2+)-dependent. The antibody bound factor IXa (K(D) = 7.6 x 10(-10) M) with about 10-fold higher affinity than factor IX (K(D) = 6.2 x 10(-9) M). Binding of the antibody to factor IXa did not affect the amidolytic activity of the protein, nor was binding affected by active site inhibition of factor IXa. These results are consistent with long-range interactions between the serine protease region and the N-terminal EGF-like module in factor IX.

Avdelning/ar

Publiceringsår

2001

Språk

Engelska

Sidor

1039-1044

Publikation/Tidskrift/Serie

Biochemical and Biophysical Research Communications

Volym

286

Issue

5

Dokumenttyp

Artikel i tidskrift

Förlag

Elsevier

Ämne

  • Biological Sciences

Status

Published

Forskningsgrupp

  • Clinical Chemistry, Malmö
  • Paediatric Hematologic Research Group

ISBN/ISSN/Övrigt

  • ISSN: 1090-2104