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

Autor: Matveeva, Evgenia G., Nelen, Marina I., Lobanov, Oleg I., Savitsky, Alexander P.
Předmět:
Zdroj: Journal of Fluorescence; Jan2003, Vol. 13 Issue 1, p79, 15p, 3 Charts, 17 Graphs
Abstrakt: 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. [ABSTRACT FROM AUTHOR]
Databáze: Complementary Index