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Identification and structural characterization of a mannose‐6‐phosphate containing oligomannosidic N ‐glycan from human erythropoietin secreted by recombinant BHK‐21 cells
Author(s) -
Nimtz Manfred,
Wray Victor,
Rüdiger Angelika,
Conradt Harald S.
Publication year - 1995
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 - 10.1016/0014-5793(95)00473-m
Subject(s) - baby hamster kidney cell , recombinant dna , glycan , glycosylation , mannose , oligosaccharide , sialidase , biochemistry , chemistry , neuraminidase , erythropoietin , chinese hamster ovary cell , glycoprotein , microbiology and biotechnology , biology , receptor , enzyme , cell , gene , endocrinology
A sialidase resistant mono‐charged N ‐glycan was isolated from glycosylation site I (Asn‐24) of recombinant human eruthropoietin expressed from baby hamster kidney (BHK‐21) cells and constituted approximately 2–4% of the oligosaccharide material at this glycosylation site. Mass spectrometry and both 1‐ and 2‐dimensional NMR techniques revealed a high mannose type structure (Man 6 ) with a phospho‐diesterbridged N‐acetylglucosamine as follows: