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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.

Antigen Binding and Effector Functions of a Chimeric Antibody with a Deletion of the C H 1 Domain and Non-Covalently Associated ϰ Chains