The occurrence of mouse-type oligosaccharides in mouse-human chimeric immunoglobulin G

Taei Matsui; Jiharu Hamako; Koh zoh Kameyama; Yoshikazu Kurosawa; Koiti Titani; Tsuguo Mizuochi

doi:10.1016/0006-291X(89)91709-9

The occurrence of mouse-type oligosaccharides in mouse-human chimeric immunoglobulin G

Taei Matsui, Jiharu Hamako, Koh zoh Kameyama, Yoshikazu Kurosawa, Koiti Titani, Tsuguo Mizuochi

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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.

Original language	English
Pages (from-to)	245-250
Number of pages	6
Journal	Biochemical and Biophysical Research Communications
Volume	164
Issue number	1
DOIs	https://doi.org/10.1016/0006-291X(89)91709-9
Publication status	Published - 16-10-1989

All Science Journal Classification (ASJC) codes

Biophysics
Biochemistry
Molecular Biology
Cell Biology

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10.1016/0006-291X(89)91709-9

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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.",

author = "Taei Matsui and Jiharu Hamako and Kameyama, {Koh zoh} and Yoshikazu Kurosawa and Koiti Titani and Tsuguo Mizuochi",

note = "Funding Information: We would like to thank Ms. Mari Kato for her excellent assistance. This work was supported in part by Grants-in-Aid Scientific Research from the Ministry of Education, Science Japan and from Fujita-Gakuen Health University.",

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T1 - The occurrence of mouse-type oligosaccharides in mouse-human chimeric immunoglobulin G

AU - Matsui, Taei

AU - Hamako, Jiharu

AU - Kameyama, Koh zoh

AU - Kurosawa, Yoshikazu

AU - Titani, Koiti

AU - Mizuochi, Tsuguo

N1 - Funding Information: We would like to thank Ms. Mari Kato for her excellent assistance. This work was supported in part by Grants-in-Aid Scientific Research from the Ministry of Education, Science Japan and from Fujita-Gakuen Health University.

PY - 1989/10/16

Y1 - 1989/10/16

N2 - 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.

AB - 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.

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The occurrence of mouse-type oligosaccharides in mouse-human chimeric immunoglobulin G

Abstract

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