Asymmetrically glycosylated IgG isolated from non-immune human sera |
| |
Authors: | I M Borel T Gentile J Angelucci R A Margni R A Binaghi |
| |
Institution: | 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. |
| |
Abstract: | 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. |
| |
Keywords: | |
|
|