Calcium binding to the first EGF-like module of human factor IX in a recombinant fragment containing residues 1-85. Mutations V46E and Q50E each manifest a negligible increase in calcium affinity
(1998) In FEBS Letters 421(2). p.100-104- Abstract
- The first EGF-like module of human coagulation factor IX contains a single functionally important calcium ion binding site. We have now shown the dissociation constant for this site to be approximately 160 microM in a recombinant protein fragment consisting of residues 1-85 in human fIX. This represents a approximately 10-fold increase in affinity as compared with the isolated EGF module (residues 46-85). The Gla module (here with Glu instead of Gla) thus increases the affinity of the EGF module calcium ion binding site. Each of two mutations, V46E and Q50E, made to investigate whether the extra negative charge would increase the affinity of the calcium binding site manifested a negligible increase in affinity.
Please use this url to cite or link to this publication:
https://lup.lub.lu.se/record/1113645
- author
- Persson, Kristina LU ; Astermark, Jan LU ; Bjork, I and Stenflo, Johan LU
- organization
- publishing date
- 1998
- type
- Contribution to journal
- publication status
- published
- subject
- keywords
- Site-directed mutagenesis, Human factor IX, Dissociation constant, Calcium binding, EGF-like module
- in
- FEBS Letters
- volume
- 421
- issue
- 2
- pages
- 100 - 104
- publisher
- Wiley-Blackwell
- external identifiers
-
- pmid:9468287
- scopus:0032498121
- ISSN
- 1873-3468
- DOI
- 10.1016/S0014-5793(97)01546-9
- language
- English
- LU publication?
- yes
- additional info
- The information about affiliations in this record was updated in December 2015. The record was previously connected to the following departments: Clinical Chemistry, Malmö (013016000), Emergency medicine/Medicine/Surgery (013240200)
- id
- 82fde253-fd4f-4a2c-ae4f-e89e95d1ee4e (old id 1113645)
- date added to LUP
- 2016-04-01 16:23:56
- date last changed
- 2022-01-28 19:23:17
@article{82fde253-fd4f-4a2c-ae4f-e89e95d1ee4e, abstract = {{The first EGF-like module of human coagulation factor IX contains a single functionally important calcium ion binding site. We have now shown the dissociation constant for this site to be approximately 160 microM in a recombinant protein fragment consisting of residues 1-85 in human fIX. This represents a approximately 10-fold increase in affinity as compared with the isolated EGF module (residues 46-85). The Gla module (here with Glu instead of Gla) thus increases the affinity of the EGF module calcium ion binding site. Each of two mutations, V46E and Q50E, made to investigate whether the extra negative charge would increase the affinity of the calcium binding site manifested a negligible increase in affinity.}}, author = {{Persson, Kristina and Astermark, Jan and Bjork, I and Stenflo, Johan}}, issn = {{1873-3468}}, keywords = {{Site-directed mutagenesis; Human factor IX; Dissociation constant; Calcium binding; EGF-like module}}, language = {{eng}}, number = {{2}}, pages = {{100--104}}, publisher = {{Wiley-Blackwell}}, series = {{FEBS Letters}}, title = {{Calcium binding to the first EGF-like module of human factor IX in a recombinant fragment containing residues 1-85. Mutations V46E and Q50E each manifest a negligible increase in calcium affinity}}, url = {{http://dx.doi.org/10.1016/S0014-5793(97)01546-9}}, doi = {{10.1016/S0014-5793(97)01546-9}}, volume = {{421}}, year = {{1998}}, }