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H (0) blood group determinant is present on soluble human L‐selectin expressed in BHK‐cells
Author(s) -
Gohlke Martin,
Mach Ulrich,
Nuck Rolf,
Volz Barbara,
Fieger Claudia,
Tauber Rudolf,
Reutter Werner
Publication year - 1999
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(99)00476-7
Subject(s) - exoglycosidase , baby hamster kidney cell , fucosylation , glycan , glycoprotein , fucose , glycosylation , recombinant dna , chemistry , biochemistry , microbiology and biotechnology , sialic acid , oligosaccharide , abo blood group system , human blood , biology , gene , immunology , physiology , cell
In the present study we show that the H (0) blood group determinant Fucα1‐2Galβ1‐4GlcNAcβ1‐R is present on N ‐linked glycans of soluble human L‐selectin recombinantly expressed in baby hamster kidney (BHK) cells. The glycans were isolated using complementary HPLC techniques and characterized by a combination of exoglycosidase digestion and mass spectrometry. The linkage of the fucose residues was determined by incubation of the glycans with specific fucosidases. The H blood determinant Fucα1‐2Galβ1‐4GlcNAcβ1 was detected for bi‐, 2,4 branched tri‐ and tetraantennary structures. To our knowledge, the proposed oligosaccharide structures represent a new glycosylation motif for recombinant glycoproteins expressed on BHK cells.