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- W2000344644 abstract "1 An autolytic endo-β-glucosaminidase, capable of cleaving the glycoside linkages of N-unsubstituted glucosamine in the glycan moiety of cell wall peptidoglycan, was purified 470-fold from a salt extract of the 20000 x g precipitate fraction obtained after sonication of a lysozyme-resistant strain of Bacillus cereus. The properties of this enzyme were studied. 2 The purified enzyme preparation was also active towards the glycan chain of fully N-acetylated cell wall peptidoglycan. 3 The endo-β-glucosaminidase was inactive towards the cell wall peptidoglycan unless the peptide portion of this polymer was removed either by the action of N-acetylmuramyl-l-alanine amidase or by the treatment with alkali in aqueous dimethyl sulfoxide. 4 Studies on the action of this enzyme towards chemically modified glycans revealed that the carboxyl groups of muramic acid residues are indispensable to a substrate for this enzyme." @default.
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- W2000344644 date "1980-11-01" @default.
- W2000344644 modified "2023-09-26" @default.
- W2000344644 title "Separation and Characterization of an Autolytic Endo-beta-glucosaminidase from Bacillus cereus" @default.
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- W2000344644 doi "https://doi.org/10.1111/j.1432-1033.1980.tb07203.x" @default.
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