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Structural changes in the N-linked sugar chains of serum immunoglobulin G of HTLV-I transgenic mice.

作者信息

Endo T, Iwakura Y, Kobata A

机构信息

Department of Biochemistry, University of Tokyo, Japan.

出版信息

Biochem Biophys Res Commun. 1993 May 14;192(3):1004-10. doi: 10.1006/bbrc.1993.1516.

DOI:10.1006/bbrc.1993.1516
PMID:8507175
Abstract

IgGs were purified from the sera of HTLV-I transgenic and nontransgenic mice. Comparative studies of the N-linked sugar chains released by hydrazinolysis revealed that their structures of transgenic IgG are quite different from those of nontransgenic IgG. Although both IgGs contained biantennary complex-type oligosaccharides, transgenic IgG had more agalactosylated forms (45%) than those from nontransgenic IgG (28%), just as was found in patients with rheumatoid arthritis (RA). Since these transgenic mice express arthritis similar to RA, it will be a useful model to investigate the relationship between the galactosylation of IgG and the development of RA.

摘要

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