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Endoglycosidases are enzymes with the ability to cleave certain N-and O- linked glycans attached to glycoproteins. The biochemical structure of some erythrocyte glycoproteins attached carbohydrate chains are not elucidate yet. The aim of this study is to investigate the effects of different endoglycosidases on three purified erythrocyte glycoproteins, CD147, CD47 and CD44, which will also provide clues about the structure of their N-linked glycans. Peptide-N-glycosidase F (PNGaseF), Endo-β-N-acetylglucosaminidase F1 (EndoF1), endo-β-N-acetylglucosaminidase H (EndoH) or Endo-β-galactosidase (Endoβ) was used to digest the glycoproteins purified by antibody high-affinity chromatography, and the results were analysed by sodium dodecyl sulfate polyacrylamide gel electrophoresis. CD147, CD47 and CD44 were purified effectively by BRIC235, BRIC126 and MA103, respectively. PNGaseF caused a significant variation in the electrophoretic mobility of the glycoproteins, while no remarkable effects of Endoβ were detected. EndoH caused a reduction in the molecular weight of CD47 and CD44, although it did not appear to cleave all the glycans. In contrast, EndoH cleaved almost all glycans from CD147. Our results indicate that most of the N-linked glycans of CD147 and CD47 are high-mannose and hybrid types. The findings suggest that a significant amount of CD44 N-glycans are from complex oligosaccharides.

The Effects of Different Endoglycosidases on Erythrocyte CD44, CD47 and CD147 Purified by Affinity Chromatography