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.
|Number of pages||7|
|Journal||Biochemical and biophysical research communications|
|Publication status||Published - 1977 Apr 25|
ASJC Scopus subject areas
- Molecular Biology
- Cell Biology