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Institute of Bioorganic Chemistry, Russian Academy of Sciences, Moscow, Russia
Abstract
[print version]

E.N.Kaliberda, V.V.Nasonov, V.K.Antonov
Deglycosylation of Glycoproteins with Glycopeptidamidase-A.
Bioorgan. Khim., 18 (4), pp. 531 - 539, (1992)

Efficiency of the releasing of N-oligosaccharides from intact or denaturated glycoproteins by the sweet almond glycopeptidamidase A has been studied with D(h)-fragment of fibrinogen, orosomucoid, horse radish peroxidase, ovalbumin as substrates. Preliminary elimination of sialic acid is necessary to deglycosylate, with this enzyme, glycoproteins having complex N-oligosaccharides. A preincubation of the glycoproteins with chaotropic salts in reducing conditions increases the efficiency of the deglycosylation. An interrelation between the hydrophobic amino acids content in the glycoprotein and the N-glycan localization at the polypeptide chain, on one hand, and the deglycosylating efficiency with glycopeptidamidase A, on the other hand, had been revealed.

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