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PMID: 1377 Published · ppublish English Journal Article Research Support, U.S. Gov't, P.H.S.

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

Journal of bacteriology ·Vol. 125 ·No. 1 ·1976-01-00 ·Pages 324-31

Yem DW, Wu HC

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.

MeSH Terms
Acetylglucosamine/pharmacology Acetylglucosaminidase/isolation & purification,metabolism Cell-Free System Escherichia coli/enzymology Glucosamine/pharmacology Glucosides/metabolism Glycopeptides/metabolism Hexosaminidases Hydrogen-Ion Concentration Molecular Weight Muramic Acids/pharmacology
Chemicals
Glucosides Glycopeptides Muramic Acids Hexosaminidases Acetylglucosaminidase Glucosamine Acetylglucosamine
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Yem D W
Wu H C
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27 references, click to expand
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Article Info
Journal
Journal of bacteriology
Abbr.
J Bacteriol
ISSN
0021-9193
DOI
10.1128/jb.125.1.324-331.1976
Published
1976-01-00
Pages
324-31
Language
English
Region
United States
NLM ID
2985120R
PMCID
PMC233366
Subset
IM
External Links
PubMed source DOI: 10.1128/jb.125.1.324-331.1976 PMC Full Text View journal details
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