Correlation between antigen-combining-site structures and functions within a panel of catalytic antibodies generated against a single transition state analog

The catalytic antibodies created against a single transition state analog exhibit high homology in the structural and biochemical properties. The haptens are attracted to the transition state stabilization and are identical to the transition state for obtaining the catalytic antibodies. The biochemical properties of six anti-haptenic phosphonate catalytic antibodies are studied to detect active site structure. The catalytic antibodies having highly homologous primary amino acid sequences contain homogeneous binding modes to the substrate or hapten.