Abstract
An apparently homogeneous preparation of the phenylalanine-sensitive 3-deoxy-D-arabino-heptulosonate-7-phosphate synthase isoenzyme from Escherichia coli was used as the antigen for antibody production in New Zealand white rabbits. The antibodies were monospecific as judged by immunodiffusion and immunoelectrophoresis. Antigen . antibody complexes maintained full enzyme activity and were inhibited by phenylalanine, indicating that neither the active site nor the feedback-inhibitor binding site is mechanistically connected to amino acid sequences which are antigenic determinants. While phenylalanine-sensitive 3-deoxy-D-arabino-heptulosonate-7-phosphate synthase could be quantitatively removed from solution by immunoprecipitation with soluble or immobilized antibodies, neither the tyrosine-sensitive nor the tryptophan-sensitive 3-deoxy-D-arabino-heptulosonate-7-phosphate synthase, the other two isoenzymes catalyzing the first step in the biosynthesis of aromatic compounds, formed any detectable complexes with the antibodies. This indicated less structural similarity than would be expected for isoenzymes. Also, the antibodies did not cross-react with 5-dehydroquinate synthase, the enzyme catalyzing the second step of the common aromatic biosynthetic pathway.
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