Jan 1, 1976

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

Journal of Bacteriology
D W Yem, H C Wu

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-nitrophenyl-beta-D-2-acetamido-2-deoxyglucopyranoside is 0.43 mM. The molecular weight of this enzyme, determined by both Sephadex gel filtration and by sodium dodecyl sulfate gel electrophoresis, is equivalent to 36,000. It is shown to be a soluble cytoplasmic enzyme. Studies on the substrate specificites of the purified enzyme indicate that this enzyme is an exo-beta-N-acetylglucosaminidase.

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Mentioned in this Paper

Beta-N-Acetylglucosaminidase
Alkalescens-Dispar Group
Glycopeptides
Glucosides
Soluble
Gel Chromatography
Cytoplasmic
Hydrolase
Glucosaminidases
Urea Measurement

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