Characterizing N-glycan Enzyme Interactions

Possible side reactions of selected enzymes (GAP, DxChe, DxPsp and β-amylase) with N-glycans were evaluated using APTS-labeled N-glycans derived from bovine standard glycoproteins ribonuclease B, fetuin, and IgG. Specifically, activity on galactose, N-acetylglucosamine, mannose, fucose and sialic acid residues was monitored. All enzyme reactions were performed as described in Section 4.4. using disodium phosphate-citrate buffer at pH 5 as the digestion buffer.

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Burock R., Cajic S., Hennig R., Buettner F.F., Reichl U, & Rapp E. (2023). Reliable N-Glycan Analysis–Removal of Frequently Occurring Oligosaccharide Impurities by Enzymatic Degradation. Molecules, 28(4), 1843.

Publication 2023

Amylase Apts Bovine Buffer Citrate Digestion Disodium phosphate Enzyme Fetuin Fucose Galactose Glycans Glycoproteins Mannose N acetylglucosamine Ribonuclease b Sialic acid

Corresponding Organization : Max Planck Institute for Dynamics of Complex Technical Systems

Other organizations : Medizinische Hochschule Hannover, Otto-von-Guericke University Magdeburg

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Variable analysis

independent variables

Enzymes (GAP, DxChe, DxPsp, and β-amylase)

dependent variables

Activity on galactose, N-acetylglucosamine, mannose, fucose, and sialic acid residues

control variables

PH 5 disodium phosphate-citrate buffer as the digestion buffer
Enzyme reactions performed as described in Section 4.4

controls

Positive control: Not specified
Negative control: Not specified

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