Abstract:
:Particulate membrane fractions from calf liver catalyze the release of glucose from GlcNAc2-Man9-Glc1-3-oligosaccharides. Maximal oligosaccharide-glucosidase activity was obtained at pH 6.2 and a detergent concentration of 0.5% Triton X-100. This activity could be distinguished from non-specific alpha-glucosidase activity on the basis of different pH-dependence and lack of activation by detergent. The relative rates for the hydrolysis of the Glc3-, Glc2-, and Glc1-oligosaccharide, estimated from the initial velocity, was 1:12:3. There is no significant difference in the enzyme activity towards free, peptide-bound, or lipid-linked oligosaccharide. Nojirimycin and 1-deoxynojirimycin were strong inhibitors of microsomal oligosaccharide-glucosidases. Hydrolysis of Glc3-oligosaccharide was inhibited by 50% at concentrations of 0.16 mM and 2 microM, respectively. Hydrolysis of the Glc2- and Glc1-oligosaccharide was inhibited to a somewhat lower extent, suggesting the presence of at least two glucosidases, one acting on Glc3- and one acting on Glc1- and Glc2-oligosaccharide.
journal_name
Biosci Repjournal_title
Bioscience reportsauthors
Hettkamp H,Bause E,Legler Gdoi
10.1007/BF01114896subject
Has Abstractpub_date
1982-11-01 00:00:00pages
899-906issue
11eissn
0144-8463issn
1573-4935journal_volume
2pub_type
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