title: [Homogeneous immunoenzyme analysis of human immunoglobulin G using horseradish peroxidase].
abstract: The author studied the steady-state kinetics of cooxidation of 4-aminoantipyrine (AAP) with phenol and its derivatives--alpha-naphthol, o- and m-acetylaminophenols--by horseradish peroxidase and its conjugate with human immunoglobulins IgG (HRP-IgG). When phenol and AAP were used as peroxidase substrates, anti-human IgG antibodies stimulated the HPR-IgG enzyme activity in the presence of excess H2O2. A homogeneous enzyme immunoassay of human IgG was developed on the basis of this stimulating effect. The kinetics of the interactions between immunological reagents was studied. In the presence of 3% polyethylene glycol 6000, a complete antibody-antigen interaction proceeds at 37 degrees for 15-20 min. The sensitivity of the enzyme immunoassay is 350 ng/ml IgG, and the dynamic detection range is 0.35-15.0 mg/ml.
authors.forename: M N
authors.initials: MN
authors.lastname: Savenkova
mesh_terms: D000675:Ampyrone / Q000378:metabolism; D006735:Horseradish Peroxidase; D006801:Humans; D007124:Immunoenzyme Techniques; D007074:Immunoglobulin G / Q000378:metabolism*; D007700:Kinetics; D010084:Oxidation-Reduction; D013379:Substrate Specificity
chemical_list: D007074:Immunoglobulin G; D000675:Ampyrone; D006735:Horseradish Peroxidase
vernacular_title: Gomogennyĭ immunofermentnyĭ analiz immunoglobulina G cheloveka s ispol'zovaniem peroksidazy khrena.