Inhibition of N-linked complex oligosaccharide formation by 1-deoxynojirimycin, an inhibitor of processing glucosidases.
Inhibition of N-linked complex oligosaccharide formation by 1-deoxynojirimycin, an inhibitor of processing glucosidases.
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DOI:
10.1016/s0021-9258(19)45358-1
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发表时间:
1982-12
期刊:
影响因子:
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通讯作者:
Brigitte Saunier;R. Kilker;Jan S. Tkaczq;Andrea Quaronill;A. Herscovics
中科院分区:
文献类型:
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作者:
Brigitte Saunier;R. Kilker;Jan S. Tkaczq;Andrea Quaronill;A. Herscovics
Glucosidase activities which remove glucose residues from GlcZMangGlcNAcz and GlclManyGlcNAcz oligosaccharides were obtained in soluble form from Saccharomyces cerevisiae X-2180 without detergent. These two enzyme activities were clearly separated from the GlcsMangGlcNAcz oligosaccharide glucosidase which was shown previously to remove the terminal glucose residue from GlcsMan9GlcNAcz oligosaccharide (Kilker, RD, Jr., Saunier, B., Tkacz, JS, and Herscovics, A.(1981) J. Biol. Chem. 256, 5299-5303) and from the a-and b-glucosidases which act on p-nitrophenylglucopyranosides. The activities with both GlcZMan9GlcNAcz and GlclMan9GlcNAcz had the same properties and were inhibited to the same extent by glucose and, of various a-and/3-linked glucose disaccharides tested, by both nigerose and maltose. In contrast, the GlcsMan9GlcNAcz oligosaccharide glucosidase was not affected by glucose, but it was inhibited by kojibiose. These results suggest that there are two specific a-glucosidases responsible for oligosaccharide processing in S. cerevisiae.