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.
|ジャーナル||Biochemical and Biophysical Research Communications|
|出版ステータス||Published - 16-10-1989|
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