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The Carbohydrate Moieties of Mouse Immunoglobulins: Composition and Evidence against a Role in Transplacental Transport¹

From the Department of Pathology, New York University Medical Center, and the Department of Pathology, Health Sciences Center, State University of New York, Stony Brook, N. Y. 11790²

Abstract

The carbohydrate composition of several mouse myeloma proteins was determined. The basic IgG glycopeptide contained five residues of N-acetyl-glucosamine, two of fucose, one of galactose and six of mannose with only occasional units having neuraminic acid. Similarities in sugar content between human and mouse IgA and IgM are noted. Glycopeptides derived from immunoglobulins were not immunogenic in rabbits and antibodies prepared against heavy chains did not appear to react against oligosaccharide determinants. Sugar-depleted immunoglobulins, prepared by the use of specific glycosidases, behaved no differently from control material in transplacental transport suggesting no major role for the sugars in this function. Data pertaining to the location of the labile disulfide bonds, roughly analogous to that for man, is presented.

Footnotes

¹ This work was supported by Research Grant CA 10637-03 from the National Cancer Institute.

² Inquiries should be made to this address.