Abstract
Antibodies to Pseudomonas testosteroni isomerase have been generated in rabbits immunized with the isomerase. Complexes between the isomerase and antibodies were characterized by double immunodiffusion and by enzymatic assays. The titre of antibodies was determined. The enzymatic activity was totally abolished with increasing antibody concentrations. Antibody-isomerase complexes were inactive. Total immunological identity was observed between the unpurified extract and the pure enzyme either free or bound to a competitive inhibitor. However, the denatured enzyme did not interact with antibodies. Antigenic identy could not be detected between the bacterial antibodies and the bovine adrenocortical isomerase from microsomes.
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