@phdthesis{oai:nagoya.repo.nii.ac.jp:00014756,
 author = {MORIWAKI, TAKAYUKI and SUGANUMA, NOBUHIKO and FURUHASHI, MADOKA and KIKKAWA, FUMITAKA and TOMODA, YUTAKA and BOIME, IRVING and NAKATA, MUNEHIRO and MIZUOCHI, TSUGUO},
 month = {Feb},
 note = {The human chorionic gonadotropin β-subunit (hCGβ) is a glycoprotein in which 12 cysteine residues pair to form six intramolecular disulfide bonds. In order to elucidate the effect of each disulfide bond on glycosylation of the molecule, we analysed structures of asparagine-linked oligosaccharides of various recombinant hCGβ produced in Chinese hamster ovary (CHO) cells: wild-type hCGβ (βWT) and mutants in which any one of the six intramolecular disulfide bonds had been disrupted by site-directed mutagenesis. SDS-PAGE analysis of βWT and these mutants before and after digestion with endoglycosidase F and H revealed structural changes in the oligosaccharide moieties of some mutants. In addition, structural analysis of oligosaccharides obtained from metabolically labeled βWT and a mutant showed that the mutant contained additional high mannose type oligosaccharides. These results suggest that elimination of a specific disulfide bond, resulting in a change in the protein conformation, disturbs the normal assembly of the mature complex type oligosaccharides in the hCGβ molecule. Abbreviations: hCGβ, human chorionic gonadotropin β-subunit; βWT, wild type hCGβ; CHO, Chinese hamster ovary; Endo-H, endoglycosidase H; Endo-F, endoglycosidase F, 名古屋大学博士学位論文 学位の種類 : 博士(医学)(論文) 学位授与年月日:平成9年2月28日 森脇崇之氏の博士論文として提出された},
 school = {名古屋大学, NAGOYA University},
 title = {Alteration of N-linked oligosaccharide structures of human chorionic gonadotropin β -subunit by disruption of disulfide bonds},
 year = {1997}
}