By F. Calabi and M.S. Neuberger (Eds.)
Our realizing of the molecular genetics of immunoglobulins has been significantly complex through the appliance of recombinant DNA know-how. This new quantity within the renowned sequence New finished Biochemistry includes 8 chapters that draw jointly studies summarising the study into immunoglobulins and the association, rearrangement and expression in their gene constitution. Molecular Genetics of Immunoglobulin can be of specific significance to these operating within the parts of genetics and molecular biology, immunology, and mobile biology.
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Extra info for Molecular Genetics of Immunoglobulin
For IgM and IgE the hinge is replaced by an extra domain. With the involvement of tail pieces, IgM and IgA are able to form polymeric molecules. IgM is found almost exclusively as a pentamer whereas IgA is found principally as a monomer or dimer. Comparison of constant domains  reveals general conserved features, such as cysteines associated with the intradomain disulphide bridge and hydrophobic residues in alternating positions characteristic of /3-pleated sheets. Comparison also allows grouping of constant domains.
IgG2 is less efficient in complement activation. IgG4 does not appear to bind C1 and does not activate complement. In other species, mouse IgG3, IgG2a and IgG2b, guinea pig IgG2, rabbit IgG, rat IgG2b, lgGl and IgG2a. bind Clq and activate complement. Mouse IgG1, guinea pig IgGl and rat IgG2c bind C l q weakly. if at all, and do not significantly activate complement [25,65,66]. g. ) but this has not been clearly demonstrated . Activated forms of C3 and C4 also bind to IgG  via covalent interaction with residues in the heavy chain of Fab.
The immunoglobulin class is determined by the nature of the heavy chain or, more precisely, by the constant part of the heavy chain. This is so because of the origin of the heavy chain gene in recombination events, as discussed in Chapter 5 . As shown in Fig. 10, IgG, IgA and IgD have a similar arrangement of three constant domains and a hinge region. For IgM and IgE the hinge is replaced by an extra domain. With the involvement of tail pieces, IgM and IgA are able to form polymeric molecules. IgM is found almost exclusively as a pentamer whereas IgA is found principally as a monomer or dimer.