Analysis of oligosaccharides involved in the asymmetrical glycosylation of IgG monoclonal antibodies.
The aim of this study is to identify the oligosaccharide residues involved in the asymmetric glycosylation of immunoglobulins. We have studied two anti-DNP monoclonal antibodies of the IgG1 isotype. Results show both qualitative and quantitative differences in the carbohydrates of both monoclonal antibodies and their fragments F(ab')2, Fab' and Fd. One of the antibodies -112D5-, which appears to be homogeneous in the Scatchard plot, has oligosaccharide residues in the L chain and in the Fd of one of the Fab'. On the other hand, 112B2 mAb, which also appears to be asymmetrically glycosylated, shows the bimodal curve characteristic of antibodies with different combining site affinities.
Morelli
L
L
CONICET, Instituto de Estudios de la Inmunidad Humoral (IDEHU), Universidad Nacional de la Plata, Argentina.
Plotkin
L
L
Leoni
J
J
Fossati
C A
CA
Margni
R A
RA
D000818:Animals; D000911:Antibodies, Monoclonal / Q000378:metabolism*; D000915:Antibody Affinity; D015153:Blotting, Western; D006031:Glycosylation; D007140:Immunoglobulin Fab Fragments / Q000378:metabolism; D007074:Immunoglobulin G / Q000378:metabolism*; D066298:In Vitro Techniques; D037102:Lectins / Q000378:metabolism; D051379:Mice; D009844:Oligosaccharides / Q000378:metabolism*; D013329:Structure-Activity Relationship
D000911:Antibodies, Monoclonal; D007140:Immunoglobulin Fab Fragments; D007074:Immunoglobulin G; D037102:Lectins; D009844:Oligosaccharides