Analysis of oligomannosyl cores of cellular glycopeptides by digestion with endo-β-N-acetylglucosaminidases

Abstract

Most of mannose-labeled glycopeptides from SV-40 transformed fibroblasts were hydrolyzed either by endo-β-N-acetylglucosaminidase D in the presence of β-galactosidase, β-N-acetylglucosaminidase and neuraminidase or by endo-β-N-acetylglucosaminidase H. The products were oligosaccharides with the probable structure of Man nGlcNAc (n=3,5,6,….). The D enzyme preferentially released smaller oligosaccharides, while the H enzyme released larger oligosaccharides. The results indicate the structural homology between oligomannosyl cores of the cellular glycopeptides and those of non-membrane glycopeptides.