title: The occurrence of mouse-type oligosaccharides in mouse-human chimeric immunoglobulin G.
abstract: 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.
authors: Institute for Comprehensive Medical Science, Fujita-Gakuen Health University School of Medicine, Aichi, Japan.
authors: T
authors: T
authors: Matsui
authors: J
authors: J
authors: Hamako
authors: K
authors: K
authors: Kameyama
authors: Y
authors: Y
authors: Kurosawa
authors: K
authors: K
authors: Titani
authors: T
authors: T
authors: Mizuochi
mesh_terms: 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*
chemical_list: D007074:Immunoglobulin G; D009844:Oligosaccharides