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Real time analysis of antibody-antigen reaction kinetics.

Malmborg Hager, Ann-Christin LU ; Michaëlsson, A. ; Ohlin, Mats LU orcid ; Jansson, B. and Borrebaeck, Carl LU (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)
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author
; ; ; and
organization
publishing date
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}},
}