Differential glycosylation of polymeric and monomeric IgM.
A small fraction of normal IgM is secreted as monomers rather than polymers. We show here that the mu chains of monomeric IgM are glycosylated differently from the mu chains of polymeric IgM and are comparable in their glycosylation to the mu chains from mutant hybridoma cell lines which produce predominantly monomeric IgM. The difference in glycosylation between monomer and polymer mu chains is due to differences in the terminal processing of their oligosaccharides. The glycosylation of the mutant mu chains is not itself responsible for the block in IgM polymer formation.
Davis
A C
AC
Department of Immunology and Medical Genetics, University of Toronto, Ontario, Canada.
Collins
C
C
Shulman
M J
MJ
D017485:1-Deoxynojirimycin; D000818:Animals; D002460:Cell Line; D004591:Electrophoresis, Polyacrylamide Gel; D005944:Glucosamine / Q000031:analogs & derivatives / Q000378:metabolism; D006031:Glycosylation; D006825:Hybridomas; D007075:Immunoglobulin M / Q000378:metabolism*; D051379:Mice; D009154:Mutation; D011108:Polymers
D007075:Immunoglobulin M; D011108:Polymers; D017485:1-Deoxynojirimycin; D005944:Glucosamine