%0 Journal Article
%T A fluorogenic probe for core-fucosylated glycan-preferred ENGase.
%A Ishii N
%A Muto H
%A Nagata M
%A Sano K
%A Sato I
%A Iino K
%A Matsuzaki Y
%A Katoh T
%A Yamamoto K
%A Matsuo I
%J Carbohydr Res
%V 523
%N 0
%D Jan 2023
%M 36435009
%F 2.975
%R 10.1016/j.carres.2022.108724
%X A fluorescence-quenching-based assay system to determine the hydrolytic activity of endo-β-N-acetylglucosaminidases (ENGases), which act on the innermost N-acetylglucosamine (GlcNAc) residue of the chitobiose segment of core-fucosylated N-glycans, was constructed using a dual-labeled fluorescent probe with a hexasaccharide structure. The fluorogenic probe was evaluated using a variety of ENGases, including Endo-M W251N mutant, Endo-F3, and Endo-S, which recognize core fucosylated N-glycans. The occurrence of a hydrolysis reaction was detected by observing an increased fluorescence intensity, ultimately allowing the ENGase activities to be easily and quantitatively evaluated, with the exception of Endo-S. The obtained results clearly indicated the substrate specificities of the examined ENGases.