title: Asymmetric Fab glycosylation in guinea-pig IgG1 and IgG2.
abstract: The presence of asymmetric antibody molecules has been investigated in both IgG1 and IgG2 subclasses of guinea-pig immunoglobulins. It was found that about 20% of the IgG1 and 10% of the IgG2 were of asymmetric type. The proportion was essentially the same in the sera of normal animals, animals hyperimmunized with dinitrophenyl-bovine gamma globulin (DNP-BGG) and Freund's adjuvant, and animals infected with Trichinella spiralis. In the case of animals immunized with DNP-BGG, no differences were observed in the proportion of asymmetric molecules between the specific antibodies and the IgG not specific for the immunizing antigen. It is concluded that the asymmetric glycosylation occurs to a different extent in each subclass and that it is not affected by the antigen specificity of the antibodies studied.
authors.affiliation: Departamento de Microbiologia, Immunologia y Biotecnologia, Facultad de Farmacia y Bioquímica, Universidad de Buenos Aires, Argentina.
authors.forename: I
authors.initials: I
authors.lastname: Malan Borel
authors.forename: T
authors.initials: T
authors.lastname: Gentile
authors.forename: J
authors.initials: J
authors.lastname: Angelucci
authors.forename: R A
authors.initials: RA
authors.lastname: Margni
authors.forename: R A
authors.initials: RA
authors.lastname: Binaghi
mesh_terms: D000818:Animals; D006031:Glycosylation; D006168:Guinea Pigs; D007140:Immunoglobulin Fab Fragments / Q000032:analysis*; D007074:Immunoglobulin G / Q000032:analysis*
chemical_list: D007140:Immunoglobulin Fab Fragments; D007074:Immunoglobulin G