A novel β‐N‐acetylglucosaminidase activity in hog gastric mucosal microsomes: Preferential hydrolysis of terminal GlcNAcß1‐3 linkages in GlcNAcß1‐3(GlcNAcß1‐6)Galß1‐GlcNAc, but GlcNAcß1‐6 linkages in GlcNAcß1‐3(GlcNAcß1‐6)Gal

Abstract
Hog gastric mucosal microsomes contain β-N-acetylgrucosaminidase activity which cleaves GlcNAcß1-3(GlcNAcß1-6)Galß1-4GlcNAc at the terminal GlcNAcß1-3Gal linkage faster than at the GlcNAcß1-6Gal bond, producing mainly GlcNAcß1-6Galß1-4GlcNAc. In a marked contrast, GlcNAcß1-3(GlcNAcß1-6)Gal is cleaved primarily at the GlcNAcß1-6Gal bond, while partial hydrolysis of GlcNAcß1-3(GlcNAcß1-6)Gal ß1-4Glc reveals similar rates of cleavage for the (1–3) and (1–6) linkages. Our data support the notion that the terminal ß1,6-linked GlcNAc unit of GlcNAcß1-3(GlcNAcß1-6)Galß1-4GlcNAc may interact with the reducing end GlcNAc unit intramolecularly in water solution.

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