[Lectin-enzyme assay as a method of estimation of immunoglobulins' glycosylation].
The mechanism of interaction of lectins with IgG molecules by the method of the lectin-enzyme assay has been described that allows to register a degree of human serum IgG molecules' glycosylation (mannosylation in case of lectin of Pisum sativum) in norm and at pathology. To detect an authentic difference in a glycosylation degree between control and pathological IgG, the wells of an ELISA plate were coated with an antibody in concentration of 1 microg/ml. Introducing alpha-D-mannose between the stages of incubation of immunoglobulin and lectin showed, that alpha-D-mannose inhibits the affinity of lectins for IgG. The preliminary incubation of lectin with IgG molecules stabilizes the activity of horseradish peroxidase, which labeled the lectins. Lectin-enzyme assay, in which Fab and Fc fragments of IgG were used, showed that lectin of Pisum sativum possesses a higher affinity for Fab regions. These findings and the glycosylation analysis of paraproteins and Bence-Jones proteins of multiple myeloma patients help to understand the details of interaction of immunoglobulins and lectins.
Petrosian
A M
AM
Britan
A V
AV
D001536:Bence Jones Protein / Q000276:immunology* / Q000652:urine; D006031:Glycosylation; D006735:Horseradish Peroxidase; D006801:Humans; D007124:Immunoenzyme Techniques / Q000379:methods*; D007141:Immunoglobulin Fc Fragments / Q000097:blood / Q000276:immunology* / Q000652:urine; D007074:Immunoglobulin G / Q000097:blood / Q000276:immunology* / Q000652:urine; D009101:Multiple Myeloma / Q000097:blood / Q000276:immunology* / Q000652:urine; D037121:Plant Lectins
D007141:Immunoglobulin Fc Fragments; D007074:Immunoglobulin G; D037121:Plant Lectins; D001536:Bence Jones Protein; D006735:Horseradish Peroxidase