Structures of the Sugar Chains of Interferon- γ Produced by Human Myelomonocyte Cell Line HBL-38
- 1 April 1989
- journal article
- research article
- Published by Oxford University Press (OUP) in The Journal of Biochemistry
- Vol. 105 (4) , 547-555
- https://doi.org/10.1093/oxfordjournals.jbchem.a122703
Abstract
Interferon-γ produced by the human myelomonocyte cell line HBL-38 contained galactose, mannose, fucose, N-acetylglucosamine, and N-acetylneuraminic acid as sugar components. Sugar chains were liberated from interferon- γ by hydrazinolysis. Free amino groups of the sugar chains were acetylated and the reducing-end sugar residues were tagged with 2-aminopyridine under new reaction conditions in which no sialic acid residue was hydrolyzed. The pyridylamino (PA-) derivatives of the sugar chains thus obtained were purified by gel filtration and reversed-phase HPLC. Seven major PA-sugar chains were isolated and the structure of each purified PA-sugar chain was identified by stepwise exoglycosidase digestion and 500-MHz 1H-NMR spectroscopy. The results indicated that the structures of the major PA-sugar chains were of the biantennary type, to which 0 to 2 mol of fucose and 1 to 2 mol of N-acetylneuraminic acid were linked as shown below.This publication has 12 references indexed in Scilit:
- Structural studies of the carbohydrate chains of human gamma-interferonEuropean Journal of Biochemistry, 1986
- Microquantitative analysis of neutral and amino sugars as fluorescent pyridylamino derivatives by high-performance liquid chromatographyAnalytical Biochemistry, 1985
- CHARACTERISTICS OF ANTIVIRAL AND ANTICELLULAR ACTIVITIES OF HUMAN RECOMBINANT INTERFERON-GAMMA1985
- Natural human interferon-gamma. Complete amino acid sequence and determination of sites of glycosylation.Journal of Biological Chemistry, 1984
- Reexamination of the Pyridylamination Used for Fluorescence Labeling of Oligosaccharides and Its Application to Glycoproteins 1The Journal of Biochemistry, 1984
- Methylation analysis of complex carbohydrates in small amounts: Capillary gas chromatography-mass fragmentography of methylalditol acetates obtained from N-glycosidically linked glycoprotein oligosaccharidesAnalytical Biochemistry, 1983
- Primary Structure of the N-Glycosidically Linked Sialoglycans of Secretory Immunoglobulins A from Human MilkEuropean Journal of Biochemistry, 1982
- Primary Structure of the Glycans from Human LactotransferrinEuropean Journal of Biochemistry, 1982
- Structural studies of the sugar chains of human parotid alpha-amylase.Journal of Biological Chemistry, 1980
- Structure of a complex asparagine bound glycopeptide from horse pancreatic ribonuclease containing (2→3) and (2→6) linked sialic acid residuesBiochemical and Biophysical Research Communications, 1978