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Mocikat, R. ; Mysliwietz, J. ; Lang, P. ; Thierfelder, S.S.

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)

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Open Access Green as soon as Postprint is submitted to ZB.

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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

Corresponding Author

ISSN (print) / ISBN 1431-6730

e-ISSN 1437-4315

Journal Biological Chemistry

Quellenangaben Volume: 374, Issue: 7, Pages: 461-465

Publisher de Gruyter

Non-patent literature Publications

Reviewing status Peer reviewed

Institute(s) Institute of Molecular Immunology (IMI)