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- W2021002255 abstract "A bacteriolytic enzyme obtained from the culture fluid of Staphylococcus aureus FDA 209P was purified to homogeneity utilizing dye-ligand affinity column chromatography, hydrophobic interaction high pressure liquid chromatography (HPLC) and hydroxyapatite HPLC. Subsequent characterizations indicated that the purified enzyme acted as endo-beta-N-acetylglucosaminidase. The molecular weight determined by sodium dodecyl sulphate polyacrylamide gel electrophoresis (SDS-PAGE) was 51,000 and the isoelectric point was higher than 10. The optimum pH for the enzyme activity on whole cells of Micrococcus luteus as a substrate was 8.0. Some heavy metal cations (Cu2+ and Zn2+) inhibited the enzyme activity at a concentration of 0.1 mM and others (Ba2+, Mg2+ and Co2+) showed a stimulating effect at a concentration of 1 mM." @default.
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- W2021002255 date "1989-10-01" @default.
- W2021002255 modified "2023-10-18" @default.
- W2021002255 title "Purification of a 51 kDa endo-β-N-acetylglucosaminidase fromStaphylococcus aureus" @default.
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- W2021002255 doi "https://doi.org/10.1111/j.1574-6968.1989.tb03635.x" @default.
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