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Department of Microbiology, Immunology, and Molecular Genetics, and Molecular Biology Institute, University of California, Los Angeles, CA 90095
It is widely appreciated that the isotype of the H chain
of the Ab molecule influences its functional properties. We have now
investigated the contribution of the isotype of the L chain to the
structural and functional properties of the Ab molecule. In these
studies, the L chain variable region of a murine anti-dansyl Ab was
joined to either human 
or 
constant region domains and expressed
with mouse-human chimeric H chains of the four human IgG isotypes. The
resulting Abs were secreted as fully assembled molecules although, as
has been previously observed, IgG4 with either or L chains was
also secreted as HL half-molecules. However, the isotype of the L chain
can influence the kinetics of intracellular assembly with IgG1,
IgG2, and IgG4 assembling more slowly than their
counterparts. The isotype of the L chain also influenced the
susceptibility of the interchain disulfide bonds to attack by reducing
agents with variable effects, depending on the isotype of the H chains.
For IgG2, but not for IgG1, -3, and -4, the isotype of the L chain
influenced the rate of clearance in mice, with IgG2 having a shorter
in vivo half-life than IgG2. Only slight differences were also
observed between and molecules in their kinetics of binding to
and dissociation from the hapten dansyl. These studies demonstrate that
the isotype of the L chain has only a slight impact on the structural
and functional properties of variable region identical
Abs.
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