Demonstration of peptide:N-glycosidase F activity in endo-beta-N-acetylglucosaminidase F preparations.
Demonstration of peptide:N-glycosidase F activity in endo-beta-N-acetylglucosaminidase F preparations.
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发表时间：
1984-09
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通讯作者：
T. Plummer;J. Elder;S. Alexander;A. W. Phelan;A. Tarentino
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作者：
T. Plummer;J. Elder;S. Alexander;A. W. Phelan;A. Tarentino
已发现来自脑膜败血黄杆菌的内切 -β-N - 乙酰氨基葡萄糖苷酶F制剂含有肽:N - 糖苷酶活性。只有第二种活性，被命名为肽:N - 糖苷酶F，能轻易地裂解胎球蛋白三天线复合糖肽的β - 天冬氨酰糖基胺键，这可由分离出相应的含天冬氨酸的无糖肽以及在还原端具有二 -N - 乙酰壳二糖基部分的完整寡糖所证明。混合物中的两种活性都能水解来自卵清蛋白的高甘露糖八糖肽，所形成产物的类型受pH值影响。在pH 4.0时，只有内切 -β-N - 乙酰氨基葡萄糖苷酶F的活性起作用，释放出八肽 - GlcNAc和寡糖 - GlcNAc。在pH 9.3时，主要的裂解是由肽:N - 糖苷酶F在糖基胺键处进行，释放出八肽和寡糖 - GlcNAc - GlcNAc。然后，后一种寡糖被内切 -β-N - 乙酰氨基葡萄糖苷酶F水解为寡糖 - GlcNAc和GlcNAc。
Endo-beta-N-acetylglucosaminidase F preparations from Flavobacterium meningosepticum have been found to contain peptide:N-glycosidase activity. Only the second activity, designated as peptide:N-glycosidase F, readily cleaves the beta-aspartylglycosylamine linkage of a fetuin triantennary complex glycopeptide, as shown by the isolation of the corresponding carbohydrate-free peptide containing aspartic acid and of an intact oligosaccharide with a di-N-acetylchitobiosyl moiety at the reducing end. Both activities in the mixture will hydrolyze a high mannose octaglycopeptide from ovalbumin, with the type of product formed being influenced by pH. At pH 4.0, only the endo-beta-N-acetylglucosaminidase F activity is functional, releasing octapeptide-GlcNAc and oligosaccharide-GlcNAc. At pH 9.3, the predominant cleavage is by peptide:N-glycosidase F at the glycosylamine bond, releasing octapeptide and oligosaccharide-GlcNAc-GlcNAc. This latter oligosaccharide is then hydrolyzed by endo-beta-N-acetylglucosaminidase F to oligosaccharide-GlcNAc plus GlcNAc.