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Antigen-binding sites dominate the surface properties of IgG antibodies

Wingren, Christer LU ; Hansson, Ulla-Britt; Magnusson, Carl G.M and Ohlin, Mats LU (1995) In Molecular Immunology 32(11). p.819-827
Abstract
A new technique, liquid-liquid partition chromatography in an aqueous polyethylene glycol-dextran two-phase system, was used to detect differences in surface properties of antibodies with different antigen-binding sites. Employing well-characterized monoclonal IgG antibodies and Fab and Fc fragments thereof as well as chimeric IgG antibodies we found a remarkable relationship between structure of the antibody combining site and chromatographic behaviour. The surface properties of the IgG antibodies were dominated by those of its antigen-binding regions. In addition, our results indicated that the constant parts of the IgGs form similar scaffoldings, on to which CDRs of variable shapes and sizes are interspaced and constitute the major... (More)
A new technique, liquid-liquid partition chromatography in an aqueous polyethylene glycol-dextran two-phase system, was used to detect differences in surface properties of antibodies with different antigen-binding sites. Employing well-characterized monoclonal IgG antibodies and Fab and Fc fragments thereof as well as chimeric IgG antibodies we found a remarkable relationship between structure of the antibody combining site and chromatographic behaviour. The surface properties of the IgG antibodies were dominated by those of its antigen-binding regions. In addition, our results indicated that the constant parts of the IgGs form similar scaffoldings, on to which CDRs of variable shapes and sizes are interspaced and constitute the major dominant differences in exposed surface properties. (Less)
Please use this url to cite or link to this publication:
author
organization
publishing date
type
Contribution to journal
publication status
published
subject
keywords
Partition chromatography, LLPC, IgG antibodies, antigen-binding sites, surface properties
in
Molecular Immunology
volume
32
issue
11
pages
819 - 827
publisher
Pergamon
external identifiers
  • scopus:0029113953
ISSN
1872-9142
DOI
10.1016/0161-5890(95)00044-F
language
English
LU publication?
yes
id
7e364147-7e27-4972-ae18-4074add3afed (old id 126540)
date added to LUP
2007-07-09 10:24:02
date last changed
2017-01-01 06:54:22
@article{7e364147-7e27-4972-ae18-4074add3afed,
  abstract     = {A new technique, liquid-liquid partition chromatography in an aqueous polyethylene glycol-dextran two-phase system, was used to detect differences in surface properties of antibodies with different antigen-binding sites. Employing well-characterized monoclonal IgG antibodies and Fab and Fc fragments thereof as well as chimeric IgG antibodies we found a remarkable relationship between structure of the antibody combining site and chromatographic behaviour. The surface properties of the IgG antibodies were dominated by those of its antigen-binding regions. In addition, our results indicated that the constant parts of the IgGs form similar scaffoldings, on to which CDRs of variable shapes and sizes are interspaced and constitute the major dominant differences in exposed surface properties.},
  author       = {Wingren, Christer and Hansson, Ulla-Britt and Magnusson, Carl G.M and Ohlin, Mats},
  issn         = {1872-9142},
  keyword      = {Partition chromatography,LLPC,IgG antibodies,antigen-binding sites,surface properties},
  language     = {eng},
  number       = {11},
  pages        = {819--827},
  publisher    = {Pergamon},
  series       = {Molecular Immunology},
  title        = {Antigen-binding sites dominate the surface properties of IgG antibodies},
  url          = {http://dx.doi.org/10.1016/0161-5890(95)00044-F},
  volume       = {32},
  year         = {1995},
}