The occurrence of mouse-type oligosaccharides in mouse-human chimeric immunoglobulin G.
The asparagine-linked sugar chains of mouse-human chimeric IgG which is composed of the variable regions derived from mouse and the constant regions derived from human and produced in mouse cells were quantitatively released as tritium-labelled oligosaccharides by hydrazinolysis followed by N-acetylation and NaB3H4-reduction. Paper electrophoresis in combination with sialidase digestion indicated that more than 70% of the oligosaccharides were neutral and the rest was sialylated oligosaccharides. Their structures were determined by sequential exoglycosidase digestions. The mouse-human chimeric IgG was shown to have same sugar chains as those of mouse IgG.
Matsui
T
T
Institute for Comprehensive Medical Science, Fujita-Gakuen Health University School of Medicine, Aichi, Japan.
Hamako
J
J
Kameyama
K
K
Kurosawa
Y
Y
Titani
K
K
Mizuochi
T
T
D000818:Animals; D002236:Carbohydrate Conformation; D055598:Chemical Phenomena; D002621:Chemistry; D002678:Chimera; D002846:Chromatography, Affinity; D002850:Chromatography, Gel; D004590:Electrophoresis, Paper; D006801:Humans; D006868:Hydrolysis; D007074:Immunoglobulin G / Q000378:metabolism*; D051379:Mice; D009844:Oligosaccharides / Q000302:isolation & purification / Q000378:metabolism*
D007074:Immunoglobulin G; D009844:Oligosaccharides