Immunochemical reactivity of native and modified preparations of pig kidney diamine oxidase.
This paper describes the antigenicity of pig kidney diamine oxidase [EC 1.4.3.6] and the possible role of constituent amino acids in the epitope structure of the enzyme. The loss of 62% of the biological activity after DAO-anti-DAO antibodies interaction was attributed to the steric hindrance caused by binding of antibody to the enzyme molecule. A gradual loss in antigenicity during ultraviolet (UV) irradiation was observed without any significant conformational change, demonstrating the destruction of antigenic determinants. However, ethoxyformylation of nine histidyl residues with complete inactivation caused no change in immunoreactivity. The results indicate that the antigenic sites and catalytic sites are located at different positions along the polypeptide chain. Moreover, the results of lysine residue modification were suggestive of possible involvement of lysine in the antigenic determinants of DAO.
Shah
M A
MA
Department of Biochemistry, Faculty of Medicine, Aligarh Muslim University, India.
Ali
R
R
D006631:Amine Oxidase (Copper-Containing) / Q000032:analysis* / Q000276:immunology; D000818:Animals; D001120:Arginine / Q000032:analysis / Q000276:immunology; D002384:Catalysis; D006639:Histidine / Q000032:analysis / Q000276:immunology; D007120:Immunochemistry; D005779:Immunodiffusion; D007074:Immunoglobulin G / Q000276:immunology; D066298:In Vitro Techniques; D007668:Kidney / Q000201:enzymology*; D008239:Lysine / Q000032:analysis / Q000276:immunology; D013056:Spectrophotometry, Ultraviolet; D013552:Swine
D007074:Immunoglobulin G; D006639:Histidine; D001120:Arginine; D006631:Amine Oxidase (Copper-Containing); D008239:Lysine