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- W2022248828 abstract "Taka-amylase A (1,4-α-d-glucan glucanohydrolase, EC 3.2.1.1), which contains a single asparagine-linked oligosaccharide unit, was digested with almond glycopeptidase immobilized on Sepharose 6B at 20°C for 4 h. A maximum of 10% of the parent protein was isolated as apoprotein by column chromatography on Con-A Sepharose. The characteristics of the apoprotein were compared to those of the native Taka-amylase A. The removal of the sugar chain from Taka-amylase A caused no change in the pH-activity profile or in kinetic parameters of the hydrolysis of soluble starch. The stability of the apoprotein toward changing pH and digestion by proteases did not show any appreciable difference from that of the native Taka-amylase. These results suggest that the carbohydrate moiety of Taka-amylase A is not an essential participant in the catalysis." @default.
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- W2022248828 date "1996-01-01" @default.
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- W2022248828 title "428 The 68 kDa human β-secretase in brains of Alzheimer's disease patients contains heparan sulfate glycoconjugate" @default.
- W2022248828 doi "https://doi.org/10.1016/s0197-4580(96)80430-1" @default.
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