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- W1524422016 abstract "Flavobacterium meningosepticum endo-beta-acetyl-glucosaminidase F preparations have been resolved by hydrophobic interaction chromatography on TSK-butyl resin into at least three activities designated endo F1, endo F2 and endo F3 each with a unique substrate specificity. The 32-kDa endo F1 protein is the principle component representing in excess of 95% of most earlier and currently available commercial endoglycosidase preparations, the remainder being a mixture of five proteins from 32 to 43 kDa. Substrate specificity studies reveal endo F1 and endo H from Streptomyces plicatus to have nearly identical capacities to hydrolyze high-mannose oligosaccharides with a minimum Man1 alpha 3Man1 alpha 6Man1 beta 4GlcNAc1 beta 4GlcNAc structure. Although endo H will hydrolyze fucose-containing hybrid oligosaccharides at rates approaching comparable high-mannose forms, core-linked fucose reduces the hydrolysis rate of endo F1 by over 50-fold relative to high-mannose structures. Neither homogeneous endo F1 nor endo H hydrolyze complex multi-antennary glycans. The biantennary cleaving activity previously reported for endo F preparations (Tarentino, A. L., Gomez, C. M., and Plummer, T. H., Jr. (1985) Biochemistry 24, 4665-4671) is a characteristic of the contaminating endo F2 activity." @default.
- W1524422016 created "2016-06-24" @default.
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- W1524422016 date "1991-01-01" @default.
- W1524422016 modified "2023-09-30" @default.
- W1524422016 title "Identification of distinct endoglycosidase (endo) activities in Flavobacterium meningosepticum: endo F1, endo F2, and endo F3. Endo F1 and endo H hydrolyze only high mannose and hybrid glycans" @default.
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- W1524422016 doi "https://doi.org/10.1016/s0021-9258(18)52343-7" @default.
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