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. Author manuscript; available in PMC: 2021 Aug 20.
Published in final edited form as: Glycobiology. 2020 Aug 20;30(9):735–745. doi: 10.1093/glycob/cwaa023

Figure III. Defucosylation of AGP N-glycans by certain GH29 members in our collection.

Figure III

a) CE-LIF profiles of an untreated control or b) after overnight incubation of isolated α1 acid glycoprotein (AGP) N-glycans with a clarified E. coli lysate containing fucosidases C11, D11, E1, E7, F11 or H6 at pH 5.5 (see Supplementary Figure S4 for the composition of these glycans). Each of these enzymes were able to, at least in part, remove the branch α1-3 fucose as found on the multiantennary N-glycans. c) Two of these hits were able to act on the AGP N-glycans while they were still attached to the glycoprotein. In all experiments, the glycans were treated with sialidase after fucosidase treatment and prior to CE-LIF analysis to simplify quantification of the branch fucose levels. Peaks containing branch fucose are highlighted in red. ESR: enzyme-substrate ratio (weight).