Asymmetrically glycosylated IgG isolated from non-immune human sera.
When human IgG or its F(ab')2 fragment purified from a pool of non-immune sera was passed through a Con A-Sepharose column, 12% of the molecules bound to concanavalin A. While 44% of Fab' and 72% of Fd' fragments obtained from F(ab')2 retained by concanavalin A and eluted with methyl alpha-D-mannoside bound to concanavalin A, the Fab' and Fd' fragments obtained from non-retained F(ab')2 and the L chains and Fc fragments did not interact with the lectin. Only Fd' fragment obtained from the F(ab')2 retained by concanavalin A inhibited the fixation of guinea-pig erythrocytes to concanavalin A. These results are similar to those previously observed for IgG antibodies of different animal species and indicate that partial asymmetric glycosylation is a general phenomenon that is not restricted exclusively to IgG molecules with known specificity.
Borel
I M
IM
Instituto de Estudios de la Inmunidad Humoral (CONICET-UBA), Departamento de Microbiología e Inmunología, Facultad de Farmacia y Bioquímica de la Universidad de Buenos Aires, Argentina.
Gentile
T
T
Angelucci
J
J
Margni
R A
RA
Binaghi
R A
RA
D000818:Animals; D006031:Glycosylation; D006168:Guinea Pigs; D006801:Humans; D007140:Immunoglobulin Fab Fragments / Q000378:metabolism; D007074:Immunoglobulin G / Q000032:analysis*; D013329:Structure-Activity Relationship
D007140:Immunoglobulin Fab Fragments; D007074:Immunoglobulin G