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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
Author(s) -
Helin Jari,
Seppo Antti,
Leppänen Anne,
Penttilä Leena,
Maaheimo Hannu,
Niemelä Ritva,
Lauri Sari,
Renkonen Ossi
Publication year - 1993
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(93)80747-i
Subject(s) - chemistry , beta (programming language) , hydrolysis , stereochemistry , glycosylation , biochemistry , glycoside hydrolase , n acetylglucosamine , beta galactosidase , cleavage (geology) , anomer , enzyme , biology , gene , gene expression , paleontology , fracture (geology) , computer science , programming language
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.