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Purification and properties of beta-N-acetylglucosaminidase from Escherichia coli

Journal of Bacteriology

Jan 1, 1976

D W Yem, H Y Grace Wu

PMID: 1377

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Abstract

beta-N-acetylglucosaminidase (EC 3.2.1.30) has been purified from Escherichia coli K-12 to near homogeneity based on polyacrylamide gel electrophoresis in both 0.5% sodium dodecyl sulfate and in 6 M urea at pH 8.5. The purified enzyme shows a pH optimum of 7.7 and the Km for p-nitrophen...read more

Mentioned in this Paper

Soluble
Cytoplasmic
Acetylglucosamine
Hydrolase
Glucosaminidases
Cell-Free System
Urea
Polyacrylamide Gel Electrophoresis
Cytoplasm
Hydrogen-Ion Concentration
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  • Purification and properties of beta-N-acetylglucosaminidase from Escherichia coli

    Journal of Bacteriology

    Jan 1, 1976

    D W Yem, H Y Grace Wu

    PMID: 1377

    DOI:

    Abstract

    beta-N-acetylglucosaminidase (EC 3.2.1.30) has been purified from Escherichia coli K-12 to near homogeneity based on polyacrylamide gel electrophoresis in both 0.5% sodium dodecyl sulfate and in 6 M urea at pH 8.5. The purified enzyme shows a pH optimum of 7.7 and the Km for p-nitrophen...read more

    Mentioned in this Paper

    Soluble
    Cytoplasmic
    Acetylglucosamine
    Hydrolase
    Glucosaminidases

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