Participation of rat immunoglobulin light chains of the kappa and lambda type in formation of antibodies to the polysaccharide of group A streptococcus

• Published in: Molekuliarnaia biologiia Vol. 12; no. 3; p. 511
• Main Authors: Krylov, M Iu, Rokhlin, O V
• Format: Journal Article
• Language: Russian
• Published: Russia (Federation) 01-05-1978
• Subjects: Acetylglucosamine - immunology; Alleles; Animals; Antibodies, Bacterial - genetics; Chemical Phenomena; Chemistry; Hybridization, Genetic; Immunoglobulin kappa-Chains - biosynthesis; Immunoglobulin lambda-Chains - biosynthesis; Immunoglobulin Light Chains - biosynthesis; Mice; Mice, Inbred Strains; Polysaccharides, Bacterial - immunology; Rats; Streptococcus pyogenes - immunology
• ISSN: 0026-8984

The role of light kappa and lambda chains and also allelic variants of kappa chains of rat immunoglobins in the formation of antibodies to beta-N-acetyl-glucosamine polysaccharides of streptococcus group A of inbred rat strains MSU, WAG, August and hybrids of the first generation (MUS X WAG)F1 and (MSU X August)F1 was studied. From individual sera of immune rats fractions of specific antibodies to beta-N-acetyl-glucosamine were isolated. These antibodies differ in their affinity to antigenes. The retio of molecules with kappa and lambda light chain types was determined for the fraction of specific antibodies. The ratio of molecules kappa and lambda depends on the affinity of antibodies to beta-N-acetyl-glucosamine and on the genotype of the animals studied. Data obtained allow to conclude that differences in the functional activity of lambda chains between strains WAG and August, on one hand, and strain MSU, on the other, do exist. Functional differences releaved between these rat strains were confirmed by analyzing corresponding antibody fractions to beta-N-acetylglucosamine in F1 hybrids. Differences between allelic variants of kappa chains in the formation of antibodies to beta-N-acetylglucosamine of polysaccharides were not found.