Studies on the active product of pepsin digestion of rabbit immunoglobulin G (IgG), F(ab′)2 produced from antiserum against Neurospora glutamate dehydrogenase, showed it to behave in the same way, in both antienzyme and precipitation experiments, as homologous IgG. It is proposed that the inhibition of glutamate dehydrogenase by this antibody preparation is by the same mechanism as proposed for IgG and Fab, a change in the configuration of the catalytic site brought about by antibodies. Antibodies prepared against two mutant proteins behaved in antienzyme studies in the same way as antibodies prepared against the wild-type protein. It is thought therefore that the antigenic sites on the mutant proteins which initiate the production of neutralizing antibodies were not affected by the mutation which had changed the catalytic properties of the mutant proteins
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