A novel beta-N-acetylglucosaminidase activity in hog gastric mucosal microsomes: preferential hydrolysis of terminal GlcNAc beta 1-3 linkages in GlcNAc beta 1-3(GlcNAc beta 1-6)Gal beta 1-4GlcNAc, but GlcNAc beta 1-6 linkages in GlcNAc beta 1-3(GlcNAc beta 1-6)Gal

• Published in: FEBS letters Vol. 335; no. 2; pp. 280 - 284
• Main Authors: Helin, J, Seppo, A, Leppänen, A, Penttilä, L, Maaheimo, H, Niemelä, R, Lauri, S, Renkonen, O
• Format: Journal Article
• Language: English
• Published: England 06.12.1993
• Subjects: Acetylglucosaminidase - metabolism; Animals; Carbohydrate Sequence; Gastric Mucosa - enzymology; Hydrolysis; In Vitro Techniques; Microsomes - enzymology; Molecular Sequence Data; Oligosaccharides - metabolism; Swine; Trisaccharides - metabolism
• ISSN: 0014-5793
• DOI: 10.1016/0014-5793(93)80747-I

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