Asymmetrically glycosylated IgG isolated from non-immune human sera

Biochim Biophys Acta. 1989 Feb 24;990(2):162-4. doi: 10.1016/s0304-4165(89)80029-7.

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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Glycosylation
  • Guinea Pigs
  • Humans
  • Immunoglobulin Fab Fragments / metabolism
  • Immunoglobulin G / analysis*
  • Structure-Activity Relationship

Substances

  • Immunoglobulin Fab Fragments
  • Immunoglobulin G