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Antigen-binding sites dominate the surface properties of antibodies

Hansson, Ulla-Britt; Wingren, Christer LU and Andersson, Kerstin (1996) In Immunotechnology 2(4). p.276-276
Abstract
We have found a remarkable relationship between the specificity of antibodies and their chromatographic behavious upon liquid-liquid partition chromatography (LLPC). Well characterized human and murine monoclonal antibodies and Fab/Fv fragments thereof as well as mouse/human chimeric antibodies were employed.

While, lgG 1, 2 and 4 antibodies with identical specificities (affinity constants) have identical partition properties, lgG antibodies with different partition properties reacted with different partition epitopes or had different affinities against the same epitope. Hence, the surface properties of the antigen binding sites dominate over all other surfaces of the free antibody molecule.

LLPC may also be used to... (More)
We have found a remarkable relationship between the specificity of antibodies and their chromatographic behavious upon liquid-liquid partition chromatography (LLPC). Well characterized human and murine monoclonal antibodies and Fab/Fv fragments thereof as well as mouse/human chimeric antibodies were employed.

While, lgG 1, 2 and 4 antibodies with identical specificities (affinity constants) have identical partition properties, lgG antibodies with different partition properties reacted with different partition epitopes or had different affinities against the same epitope. Hence, the surface properties of the antigen binding sites dominate over all other surfaces of the free antibody molecule.

LLPC may also be used to detect conformational changes occuring upon binding of antigen by antibody. Antigen-antibody complexes formed by different lgG antibodies against a large antigen like HSA all had similar surface properties. different from those of both antigen and antibody. In contrast, the surface properties of complexes formed by small antigens haptens are related to those of the lgG antibody.

In addition, antigen-antibody complexes were found to have similar surface properties irrespective of the molar ratio of antigen to antibody at which the complexes had been formed. (Less)
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author
organization
publishing date
type
Contribution to journal
publication status
published
subject
in
Immunotechnology
volume
2
issue
4
pages
276 - 276
publisher
Elsevier
ISSN
1380-2933
DOI
10.1016/S1380-2933(97)89006-9
language
English
LU publication?
yes
id
6f58a1d9-6838-45de-9994-8787695ae9ed (old id 126276)
date added to LUP
2007-07-05 13:40:19
date last changed
2016-04-20 09:44:02
@article{6f58a1d9-6838-45de-9994-8787695ae9ed,
  abstract     = {We have found a remarkable relationship between the specificity of antibodies and their chromatographic behavious upon liquid-liquid partition chromatography (LLPC). Well characterized human and murine monoclonal antibodies and Fab/Fv fragments thereof as well as mouse/human chimeric antibodies were employed.<br/><br>
While, lgG 1, 2 and 4 antibodies with identical specificities (affinity constants) have identical partition properties, lgG antibodies with different partition properties reacted with different partition epitopes or had different affinities against the same epitope. Hence, the surface properties of the antigen binding sites dominate over all other surfaces of the free antibody molecule.<br/><br>
LLPC may also be used to detect conformational changes occuring upon binding of antigen by antibody. Antigen-antibody complexes formed by different lgG antibodies against a large antigen like HSA all had similar surface properties. different from those of both antigen and antibody. In contrast, the surface properties of complexes formed by small antigens haptens are related to those of the lgG antibody.<br/><br>
In addition, antigen-antibody complexes were found to have similar surface properties irrespective of the molar ratio of antigen to antibody at which the complexes had been formed.},
  author       = {Hansson, Ulla-Britt and Wingren, Christer and Andersson, Kerstin},
  issn         = {1380-2933},
  language     = {eng},
  number       = {4},
  pages        = {276--276},
  publisher    = {Elsevier},
  series       = {Immunotechnology},
  title        = {Antigen-binding sites dominate the surface properties of antibodies},
  url          = {http://dx.doi.org/10.1016/S1380-2933(97)89006-9},
  volume       = {2},
  year         = {1996},
}