Characterization of a monoclonal antibody to Mycobacterium kansasii.
The characterization of an IgG2/Kappa monoclonal antibody against a protein antigen obtained by gel chromatography of the complex sonicate of M. kansasii biomass is described. It recognized specifically epitope molecules in complex and fractionated M. kansasii antigens ranging from 14.4 to 20 kD. The 20 kD immunoreactive band is common to the complex antigen, its fraction A and to the fraction B which was employed as the immunogenic agent. The 14.4 and 18 kD bands are predominantly present in the fraction B. High dilution of this MoAb (1:200,000) employed successfully in immunoblot studies suggests an antibody of very high affinity which could be useful for affinity purification of mycobacterial antigens in serodiagnosis of mycobacterial infections and in demonstration of antigens in biological materials.
Wisingerová
E
E
Institute of Hygiene and Epidemiology, Prague, Czechoslovakia.
Janota
J
J
Havelková
M
M
Kubín
M
M
D000911:Antibodies, Monoclonal / Q000276:immunology*; D000942:Antigens, Bacterial / Q000276:immunology / Q000302:isolation & purification*; D004591:Electrophoresis, Polyacrylamide Gel; D000939:Epitopes / Q000032:analysis*; D007074:Immunoglobulin G / Q000276:immunology; D007145:Immunoglobulin kappa-Chains / Q000276:immunology; D008970:Molecular Weight; D009161:Mycobacterium / Q000276:immunology*; D013045:Species Specificity
D000911:Antibodies, Monoclonal; D000942:Antigens, Bacterial; D000939:Epitopes; D007074:Immunoglobulin G; D007145:Immunoglobulin kappa-Chains