An anti-EGF monoclonal antibody that detects intramolecular communication in factor IX
(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)
Please use this url to cite or link to this publication:
https://lup.lub.lu.se/record/1122843
- author
- Persson, Kristina LU ; Knobe, Karin LU and Stenflo, Johan LU
- organization
- publishing date
- 2001
- 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
- 10.1006/bbrc.2001.5398
- language
- English
- LU publication?
- yes
- id
- 1b552e7e-0504-47ff-aac8-b03de60b547f (old id 1122843)
- date added to LUP
- 2016-04-01 16:03:44
- date last changed
- 2022-01-28 17:00:49
@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/10.1006/bbrc.2001.5398}}, doi = {{10.1006/bbrc.2001.5398}}, volume = {{286}}, year = {{2001}}, }