A NOVEL BETA-N-ACETYLGLUCOSAMINIDASE ACTIVITY IN HOG GASTRIC-MUCOSAL MICROSOMES - PREFERENTIAL HYDROLYSIS OF TERMINAL GLCNAC-BETA-1-3 LINKAGES IN LCNAC-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

Authors
HELIN J SEPPO A LEPPANEN A PENTTILA L MAAHEIMO H NIEMELA R LAURI S RENKONEN O
Citation
J. Helin et al., A NOVEL BETA-N-ACETYLGLUCOSAMINIDASE ACTIVITY IN HOG GASTRIC-MUCOSAL MICROSOMES - PREFERENTIAL HYDROLYSIS OF TERMINAL GLCNAC-BETA-1-3 LINKAGES IN LCNAC-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, FEBS letters, 335(2), 1993, pp. 280-284
Citations number
11
Categorie Soggetti
Biophysics,Biology
Journal title
FEBS letters → ACNP
ISSN journal
00145793
Volume
335
Issue
2
Year of publication
1993
Pages
280 - 284
Database
ISI
SICI code
0014-5793(1993)335:2<280:ANBAIH>2.0.ZU;2-#
Abstract
Hog gastric mucosal microsomes contain beta-N-acetylglucosaminidase ac tivity which cleaves GlcNAc beta 1-3(GlcNAc beta 1-6)Gal beta 1-4GlcNA c 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 not ion that the terminal beta 1,6-linked GlcNAc unit of GlcNAc beta 1-3(G lcNAc beta 1-6)Gal beta 1-4GlcNAc may interact with the reducing end G lcNAc unit intramolecularly in water solution.