Skip to main content
Article thumbnail
Location of Repository

Immunochemical Studies on Glutamate Dehydrogenase and on Two Mutant Forms of the Protein1

By David B. Roberts


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

Topics: Infection and Immunity
Year: 1967
OAI identifier:
Provided by: PubMed Central
Sorry, our data provider has not provided any external links therefore we are unable to provide a link to the full text.

Suggested articles

To submit an update or takedown request for this paper, please submit an Update/Correction/Removal Request.