Real time analysis of antibody-antigen reaction kinetics.
(1992) In Scandinavian Journal of Immunology 35(6). p.643-650- Abstract
- Surface plasmon resonance, i.e. detection of changes in refractive index on a surface, was used in a biosensor to evaluate the dissociation/association rate and affinity constants of human monoclonal IgG and IgM antibodies and Tab fragments. The results showed that an observed difference in affinity constants between intact and fragmented IgG anti-tetanus antibody was related to approximately 10-fold differences in dissociation rate constants, since the association rate constants were in the same range, i.e. 2–3×105 (m-1s-1). Affinity constants, as determined by conventional solid phase enzyme immunoassays, were substantially higher than the constants produced by the biosensor. Human monoclonal IgM anti-Tnα... (More)
- Surface plasmon resonance, i.e. detection of changes in refractive index on a surface, was used in a biosensor to evaluate the dissociation/association rate and affinity constants of human monoclonal IgG and IgM antibodies and Tab fragments. The results showed that an observed difference in affinity constants between intact and fragmented IgG anti-tetanus antibody was related to approximately 10-fold differences in dissociation rate constants, since the association rate constants were in the same range, i.e. 2–3×105 (m-1s-1). Affinity constants, as determined by conventional solid phase enzyme immunoassays, were substantially higher than the constants produced by the biosensor. Human monoclonal IgM anti-Tnα antibodies showed, furthermore, one order of magnitude higher association rate constants, as compared with the IgG antibodies, but since the dissociation rate constants were more than ten times higher, the resulting affinity constants of the anti-carbohydrate IgM antibodies were still somewhat lower than those of the IgG antibodies. (Less)
Please use this url to cite or link to this publication:
https://lup.lub.lu.se/record/ff2cf506-6e34-4717-abc4-b10d8bf199b1
- author
- Malmborg Hager, Ann-Christin LU ; Michaëlsson, A. ; Ohlin, Mats LU ; Jansson, B. and Borrebaeck, Carl LU
- organization
- publishing date
- 1992
- type
- Contribution to journal
- publication status
- published
- subject
- in
- Scandinavian Journal of Immunology
- volume
- 35
- issue
- 6
- pages
- 643 - 650
- publisher
- Wiley-Blackwell
- external identifiers
-
- scopus:0026703444
- ISSN
- 0300-9475
- DOI
- 10.1111/j.1365-3083.1992.tb02970.x
- language
- English
- LU publication?
- yes
- id
- ff2cf506-6e34-4717-abc4-b10d8bf199b1
- date added to LUP
- 2022-12-05 08:46:46
- date last changed
- 2022-12-07 12:51:24
@article{ff2cf506-6e34-4717-abc4-b10d8bf199b1, abstract = {{Surface plasmon resonance, i.e. detection of changes in refractive index on a surface, was used in a biosensor to evaluate the dissociation/association rate and affinity constants of human monoclonal IgG and IgM antibodies and Tab fragments. The results showed that an observed difference in affinity constants between intact and fragmented IgG anti-tetanus antibody was related to approximately 10-fold differences in dissociation rate constants, since the association rate constants were in the same range, i.e. 2–3×10<sup>5</sup> (m<sup>-1</sup>s<sup>-1</sup>). Affinity constants, as determined by conventional solid phase enzyme immunoassays, were substantially higher than the constants produced by the biosensor. Human monoclonal IgM anti-Tnα antibodies showed, furthermore, one order of magnitude higher association rate constants, as compared with the IgG antibodies, but since the dissociation rate constants were more than ten times higher, the resulting affinity constants of the anti-carbohydrate IgM antibodies were still somewhat lower than those of the IgG antibodies.}}, author = {{Malmborg Hager, Ann-Christin and Michaëlsson, A. and Ohlin, Mats and Jansson, B. and Borrebaeck, Carl}}, issn = {{0300-9475}}, language = {{eng}}, number = {{6}}, pages = {{643--650}}, publisher = {{Wiley-Blackwell}}, series = {{Scandinavian Journal of Immunology}}, title = {{Real time analysis of antibody-antigen reaction kinetics.}}, url = {{http://dx.doi.org/10.1111/j.1365-3083.1992.tb02970.x}}, doi = {{10.1111/j.1365-3083.1992.tb02970.x}}, volume = {{35}}, year = {{1992}}, }