Abstract
By extensive glycosidase digestion, most of carbohydrates were removed from IgG antibody against sheep erythrocytes without impairing hemagglutinating activity. The sugar-depleted IgG significantly lost the activities in antibody-dependent cell-mediated cytotoxicity, rosette formation and complement-dependent hemolysis. The results indicated the requirement of the carbohydrate moieties in recognition by Fc receptor and complement. Furthermore differential glycosidase digestion suggested that N-acetylglucosamine or mannose was the key sugar residue required for the maintenance of the activities.
| Original language | English |
|---|---|
| Pages (from-to) | 838-844 |
| Number of pages | 7 |
| Journal | Biochemical and biophysical research communications |
| Volume | 75 |
| Issue number | 4 |
| DOIs | |
| Publication status | Published - 1977 Apr 25 |
ASJC Scopus subject areas
- Biophysics
- Biochemistry
- Molecular Biology
- Cell Biology
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Cite this
Koide, N., Nose, M., & Muramatsu, T. (1977). Recognition of IgG by Fc receptor and complement: Effects of glycosidase digestion. Biochemical and biophysical research communications, 75(4), 838-844. https://doi.org/10.1016/0006-291X(77)91458-9