Open AccessStructural studies of the carbohydrate chains of human γ‐interferon
Author(s) -
MUTSAERS Johanna H. G. M.,
KAMERLING Johannis P.,
DEVOS Rene,
GUISEZ Yves,
FIERS Walter,
VLIEGENTHART Johannes F. G.
Publication year - 1986
Publication title -
european journal of biochemistry
Language(s) - English
Resource type - Journals
eISSN - 1432-1033
pISSN - 0014-2956
DOI - 10.1111/j.1432-1033.1986.tb09627.x
Subject(s) - chinese hamster ovary cell , sialic acid , carbohydrate , glycoprotein , chemistry , oligosaccharide , biochemistry , glycosylation , stereochemistry , molar ratio , catalysis , receptor
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 1 H‐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.