Open AccessThe N‐and O‐linked carbohydrate chains of human, bovine and porcine plasminogen
Author(s) -
MARTI Thomas,
SCHALLER Johann,
RICKLI Egon E.,
SCHMID Karl,
KAMERLING Johannis P.,
GERWIG Gerrit J.,
HALBEEK Herman,
VLIEGENTHART Johannes F. G.
Publication year - 1988
Publication title -
european journal of biochemistry
Language(s) - English
Resource type - Journals
eISSN - 1432-1033
pISSN - 0014-2956
DOI - 10.1111/j.1432-1033.1988.tb13966.x
Subject(s) - glycan , sialic acid , fucosylation , chemistry , biochemistry , residue (chemistry) , carbohydrate , molar ratio , n acetylneuraminic acid , stereochemistry , glycoprotein , catalysis
The structures of the N ‐and O ‐glycans of human, bovine and porcine plasminogen were determined by 500‐MHz 1 H‐NMR spectroscopy. The N ‐glycans of all three species proved to be of the N ‐acetyllactosamine type differing from one another with respect to the sialylation and fucosylation patterns. In the N ‐glycan of human plasminogen the two antennae are sialylated with N ‐acetylneuraminic acid (NeuAc), whereas in the bovine counterpart both branches carry significant amounts of N ‐glycolylneuraminic acid (NeuGc). In porcine plasminogen the sialic acid is mainly NeuAc; the Manα1→6 branch, however, is only partially sialylated. In addition, the porcine N ‐glycan is fucosylated to about 80% in α1→6 linkage to the GlcNAc‐1 residue. The O ‐glycans of the three species possess an identical Galβ1→3GalNAc core which is α2→3 sialylated with NeuAc at Gal. The disialylated form, which is also present in all three species, has an additional NeuAc residue in α2→6 linkage to GalNAc. Mono‐and disialylated forms occur in different molar ratios in the different plasminogens: 80:20 in human, 70:30 in bovine and 50:50 in porcine. This study on the carbohydrate moiety of these three plasminogens reveals species specificity in terms of various types of microheterogeneities.