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Antigen binding and effector functions of a chimeric antibody with a deletion of the CH1 domain and non-covalently associated kappa chains.
Biol. Chem. 374, 461-465 (1993)
In a mouse/human chimeric IgG1 Ab with a deletion of the CH1 domain the disulfide bridges between H and L chain cannot be formed, although the corresponding cysteine residues are present. We show that the kappa chains are non-covalently associated to H chain dimers and that they can dissociate from the H chains. Therefore different populations of Ab can be distinguished according to the number of associated kappa chains. Only the molecules with two kappa chains can bind to the target cell. Since this Ab was derived from a T cell depleting anti-Thy-1.2 Ab, we can assess the implications of this conformational alteration as to binding avidity, effector functions and immunosuppression in vivo.
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Publication type
Article: Journal article
Document type
Scientific Article
Language
english
Publication Year
1993
HGF-reported in Year
0
ISSN (print) / ISBN
1431-6730
e-ISSN
1437-4315
Journal
Biological Chemistry
Quellenangaben
Volume: 374,
Issue: 7,
Pages: 461-465
Publisher
de Gruyter
Reviewing status
Peer reviewed
Institute(s)
Institute of Molecular Immunology (IMI)
POF-Topic(s)
30504 - Mechanisms of Genetic and Environmental Influences on Health and Disease
Research field(s)
Immune Response and Infection
PSP Element(s)
G-501700-006
Scopus ID
0027630874
PubMed ID
7692879
Erfassungsdatum
1993-07-30