caa a22 4500 469115289 CHVBK 20180323133123.0 cr unu---uuuuu 170328e19920801xx s 000 0 eng 10.1007/BF00731167 doi (NATIONALLICENCE)springer-10.1007/BF00731167 Comparison of the carbohydrate moieties of recombinant soluble Fcε receptor (sFcε RII/sCD23) expressed in Saccharomyces cerevisiae and Chinese hamster ovary cells. Different O-glycosylation sites are used by yeast and mammalian cells [Elektronische Daten] [Inge Kalsner, Franz-Josef Schneider, Rudolf Geyer, Horst Ahorn, Ingrid Maurer-Fogy] Recombinant human soluble low affinity receptor for the Fc portion of IgE (sFcεRII/sCD23) was produced inSaccharomyces cerevisiae or Chinese hamster ovary cells and subjected to carbohydrate analysis. Applied methods included analytical SDS-PAGE, reversed phase HPLC, methylation analysis and sequential degradation with exoglycosidases. The results revealed that sFcεRII derived from Chinese hamster ovary cells is glycosylated exclusively at Ser-147, containing mainly the trisaccharide Sia(α2-3)Gal(β1-3)GalNAc, whereas the yeast derived glycoprotein was glycosylated at Ser-167 and contained only α-mannosyl residues. It is shown here for the first time that different amino acids of a given protein can be O-glycosylated when expressed in yeast or Chinese hamster ovary cells. Chapman & Hall, 1992 O-glycosylation in yeast nationallicence O-glycosylation in CHO cells nationallicence soluble FcεRII nationallicence methylation analysis nationallicence sequential degradation with exoglycosidases nationallicence Kalsner Inge Ernst Boehringer Institut für Arzneimittelforschung, Bender & Co Ges mbH, Dr. Boehringer Gasse 5-11, A-1121, Vienna, Austria aut Schneider Franz-Josef Ernst Boehringer Institut für Arzneimittelforschung, Bender & Co Ges mbH, Dr. Boehringer Gasse 5-11, A-1121, Vienna, Austria aut Geyer Rudolf Biochemisches Institut am Klinikum der Universität Gieβen, FriedrichstraβE 24, W-6300, Gieβen, Germany aut Ahorn Horst Ernst Boehringer Institut für Arzneimittelforschung, Bender & Co Ges mbH, Dr. Boehringer Gasse 5-11, A-1121, Vienna, Austria aut Maurer-Fogy Ingrid Ernst Boehringer Institut für Arzneimittelforschung, Bender & Co Ges mbH, Dr. Boehringer Gasse 5-11, A-1121, Vienna, Austria aut Glycoconjugate Journal Kluwer Academic Publishers 9/4(1992-08-01), 209-216 0282-0080 9:4<209 1992 9 10719 https://doi.org/10.1007/BF00731167 text/html Onlinezugriff via DOI 1 research-article jats NATIONALLICENCE 856 40 https://doi.org/10.1007/BF00731167 text/html Onlinezugriff via DOI NATIONALLICENCE 700 1- Kalsner Inge Ernst Boehringer Institut für Arzneimittelforschung, Bender & Co Ges mbH, Dr. Boehringer Gasse 5-11, A-1121, Vienna, Austria aut NATIONALLICENCE 700 1- Schneider Franz-Josef Ernst Boehringer Institut für Arzneimittelforschung, Bender & Co Ges mbH, Dr. Boehringer Gasse 5-11, A-1121, Vienna, Austria aut NATIONALLICENCE 700 1- Geyer Rudolf Biochemisches Institut am Klinikum der Universität Gieβen, FriedrichstraβE 24, W-6300, Gieβen, Germany aut NATIONALLICENCE 700 1- Ahorn Horst Ernst Boehringer Institut für Arzneimittelforschung, Bender & Co Ges mbH, Dr. Boehringer Gasse 5-11, A-1121, Vienna, Austria aut NATIONALLICENCE 700 1- Maurer-Fogy Ingrid Ernst Boehringer Institut für Arzneimittelforschung, Bender & Co Ges mbH, Dr. Boehringer Gasse 5-11, A-1121, Vienna, Austria aut NATIONALLICENCE 773 0- Glycoconjugate Journal Kluwer Academic Publishers 9/4(1992-08-01), 209-216 0282-0080 9:4<209 1992 9 10719 Metadata rights reserved Springer special CC-BY-NC licence nationallicence BK010053 XK010053 XK010000 NATIONALLICENCE NATIONALLICENCE NL-springer