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- W2000968847 abstract "β-N-Acetylaminoglucohydrolase (β-2-acetylamino-2-deoxy-D-glucoside acetylaminodeoxyglucohydrolase, EC 3.2.1.30) was extracted from malted barley and purified. The partially purified preparation was free from α-and β-glucosidase, α- and β-galactosidase, α-mannosidase and β-mannosidase. This preparation was free from α-mannosidase only after affinity chromatography with p-amino-N-acetyl-β-D-glucosaminidine coupled to Sepharose. The enzyme was active between pH 3 and 6.5 and had a pH optimum at pH 5. A MW of 92000 was obtained by sodium dodecyl sulfate-acrylamide gel electrophoresis and a sedimentation coefficient of 4.65 was obtained from sedimentation velocity experiments. β-N-Acetylaminoglucohydrolase had a Km of 2.5 × 10−4 M using the p-nitrophenyl N-acetyl β-D-glucosaminidine as the substrate." @default.
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- W2000968847 date "1976-01-01" @default.
- W2000968847 modified "2023-10-16" @default.
- W2000968847 title "Purification and properties of a β-N-acetylaminoglucohydrolase from malted barley" @default.
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- W2000968847 doi "https://doi.org/10.1016/s0031-9422(00)88833-0" @default.
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