Specific Interaction of Coproporphyrin I with Antibodies in Water and Reverse Micelles: Dimerization of Antibodies Affects Antigen Binding Site

The antigen-antibody interaction between coproporphyrin I and anti-coproporphyrin antibodies was studied by a fluorescence method in water and a reverse micellar system: n-octane/Aerosol OT. Coproporphyrin fluorescence was quenched, and coproporphyrin emission maximum was shifted to the long-wavelength region after binding to the antibodies or Fab-fragments. The mechanism of this quenching is static, most probably, by a tryptophan residue (or maybe lysine or methionine). Apparent dynamic quenching, in this case, arises from protein backbone motion. A special kind of antibody Fab-Fab dimerization was proposed.