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Rat C regions mu, gamma 1, gamma 2a, gamma 2b, gamma 2c, epsilon, and alpha have been characterized by means of chimeric antibody technology. A set of rat/mouse Ag-specific (anti-4-hydroxy-3-nitrophenacetyl) antibodies was constructed that differ only in the H chain constant region but carry identical V region and L chain, both of which are of mouse origin. All rat constant regions could be expressed and m.w. were as expected from the protein sequence. A slight variation in mobility within the IgG subclasses allowed us to establish a hierarchy for the sizes of the four gamma H chains; gamma 2b greater than gamma 1 greater than gamma 2c greater than gamma 2a. Rat IgG2c and IgG2b could be purified on both protein A and protein G while rat IgG2a could only be purified on protein G. Rat IgM and IgG2b were the most potent in C-mediated hemolysis. This was not simply a consequence of the amount of C1q bound because IgG2c bound C1q efficiently but was relatively poor in cell lysis. In ADCC using human effector and target cells, IgG2b and IgG1 were the most effective.


Journal article


J Immunol

Publication Date





3145 - 3150


Animals, Antibody-Dependent Cell Cytotoxicity, Bacterial Proteins, Binding Sites, Antibody, Chimera, Hemolysis, Hyaluronan Receptors, Immunoglobulin A, Immunoglobulin Constant Regions, Immunoglobulin E, Immunoglobulin G, Immunoglobulin Heavy Chains, Immunoglobulin Isotypes, Immunoglobulin M, Membrane Glycoproteins, Mice, Mitochondrial Proteins, Molecular Weight, Rats, Receptors, Complement, Recombinant Proteins, Staphylococcal Protein A