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

Persson, Kristina LU ; Knobe, Karin LU and Stenflo, Johan LU (2001) In Biochemical and Biophysical Research Communications 286(5). p.1039-1044
Abstract
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... (More)
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. (Less)
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author
organization
publishing date
type
Contribution to journal
publication status
published
subject
in
Biochemical and Biophysical Research Communications
volume
286
issue
5
pages
1039 - 1044
publisher
Elsevier
external identifiers
  • pmid:11527405
  • scopus:0034811245
ISSN
1090-2104
DOI
language
English
LU publication?
yes
id
1b552e7e-0504-47ff-aac8-b03de60b547f (old id 1122843)
date added to LUP
2008-07-09 11:07:37
date last changed
2018-05-29 11:30:43
@article{1b552e7e-0504-47ff-aac8-b03de60b547f,
  abstract     = {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.},
  author       = {Persson, Kristina and Knobe, Karin and Stenflo, Johan},
  issn         = {1090-2104},
  language     = {eng},
  number       = {5},
  pages        = {1039--1044},
  publisher    = {Elsevier},
  series       = {Biochemical and Biophysical Research Communications},
  title        = {An anti-EGF monoclonal antibody that detects intramolecular communication in factor IX},
  url          = {http://dx.doi.org/},
  volume       = {286},
  year         = {2001},
}