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:
https://lup.lub.lu.se/record/126540
- author
- Wingren, Christer
LU
; Hansson, Ulla-Britt
; Magnusson, Carl G.M
and Ohlin, Mats
LU
- organization
- publishing date
- 1995
- 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 Press Ltd.
- 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
- 2016-04-01 16:03:26
- date last changed
- 2021-01-03 04:53:58
@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}},
keywords = {{Partition chromatography; LLPC; IgG antibodies; antigen-binding sites; surface properties}},
language = {{eng}},
number = {{11}},
pages = {{819--827}},
publisher = {{Pergamon Press Ltd.}},
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}},
doi = {{10.1016/0161-5890(95)00044-F}},
volume = {{32}},
year = {{1995}},
}