TY - JOUR
T1 - Dynamics of the carbohydrate chains attached to the Fc portion of immunoglobulin G as studied by NMR spectroscopy assisted by selective 13C labeling of the glycans
AU - Yamaguchi, Yoshiki
AU - Kato, Koichi
AU - Shindo, Mitsuru
AU - Aoki, Shin
AU - Furusho, Kumiko
AU - Koga, Kenji
AU - Takahashi, Noriko
AU - Arata, Yoji
AU - Shimada, Ichio
N1 - Funding Information:
We thank Drs T. Terao and J. Sawada (National Institute of Health Sciences) for generously providing us with the cell line 7D7. We also thank H. Araki for HPLC analyses of the oligosaccharides used in the present study. This research was supported in part by a grant from the Japan Society for the Promotion of Science (JSPS-RFTF96L00505) and by a Grant-in-Aid for Scientific Research from the Ministry of Education, Sciences, Culture and Sports of Japan (06276102).
PY - 1998
Y1 - 1998
N2 - A systematic method for 13C labeling of the glycan of immunoglobulin G for NMR study has been developed. A mouse immunoglobulin of subclass IgG2b has been used for the experiment. On the basis of chemical shift and linewidth data, it has been concluded that (1) the mobility of the carbohydrate chain in IgG2b is comparable to that of the backbone polypeptide chain with the exception of the galactose residue at the nonreducing end of the Manα1-3 branch, which is extremely mobile and (2) agalactosylation does not induce any significant change in the mobility. The results obtained indicate that even in the agalactosyl form the glycans are buried in the protein. Biological significance of the NMR results obtained is also briefly discussed.
AB - A systematic method for 13C labeling of the glycan of immunoglobulin G for NMR study has been developed. A mouse immunoglobulin of subclass IgG2b has been used for the experiment. On the basis of chemical shift and linewidth data, it has been concluded that (1) the mobility of the carbohydrate chain in IgG2b is comparable to that of the backbone polypeptide chain with the exception of the galactose residue at the nonreducing end of the Manα1-3 branch, which is extremely mobile and (2) agalactosylation does not induce any significant change in the mobility. The results obtained indicate that even in the agalactosyl form the glycans are buried in the protein. Biological significance of the NMR results obtained is also briefly discussed.
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U2 - 10.1023/A:1008392229694
DO - 10.1023/A:1008392229694
M3 - Article
C2 - 9835046
AN - SCOPUS:0032176417
SN - 0925-2738
VL - 12
SP - 385
EP - 394
JO - Journal of Biomolecular NMR
JF - Journal of Biomolecular NMR
IS - 3
ER -