Structural studies of the carbohydrate chains of human γ‐interferon

• Published in: European journal of biochemistry Vol. 156; no. 3; pp. 651 - 654
• Main Authors: MUTSAERS, Johanna H. G. M., KAMERLING, Johannis P., DEVOS, Rene, GUISEZ, Yves, FIERS, Walter, VLIEGENTHART, Johannes F. G.
• Format: Journal Article
• Language: English
• Published: Oxford, UK Blackwell Publishing Ltd 02.05.1986; Blackwell
• Subjects: Animals; Applied sciences; Carbohydrates - analysis; Cell Line; Chemical Phenomena; Chemistry; Chromatography, Ion Exchange; Cricetinae; Cricetulus; Exact sciences and technology; Female; Humans; Hydrazines; Interferon-gamma; Magnetic Resonance Spectroscopy; N-Acetylneuraminic Acid; Other techniques and industries; Ovary; Recombinant Proteins; Sialic Acids
• ISSN: 0014-2956; 1432-1033
• DOI: 10.1111/j.1432-1033.1986.tb09627.x

Human γ‐interferon (IFN‐γ) was prepared biotechnologically using Chinese hamster ovary cells. These cells were shown to be able to produce glycosylated IFN‐γ. Sugar analysis revealed the presence of Man, Gal, GlcNAc, NeuAc and Fuc residues in a molar ratio of 3.8:2.0:3.5:0.6:0.4 suggesting the occurrence of N‐glycosidically linked N‐acetyllactosamine type of carbohydrate chains. For structure determination of these chains, the glycoprotein was subjected to the hydrazinolysis procedure, yielding oligosaccharide‐alditols. The latter compounds were analysed by 500‐MHz 1H‐NMR spectroscopy. The carbohydrate material was found to consist of biantennary structures, exhibiting microheterogeneity as to the terminal sialic acids and the core Fuc residue: As similar carbohydrates are present on several human secreted proteins, this glycosyl group is not expected to be immunogenic in man. It remains to be established to what extent the carbohydrate chains of this biotechnologically produced IFN‐γ are identical to those of naturally occurring human IFN‐γ.