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- W2070507528 abstract "Staphylococcus aureus, strain M18, produces extracellular bacterial cell wall degrading enzymes of three different classes: endo-β-N-acetylglucosaminidase, endopeptidase, and N-acetylmuramyl-L-alanine amidase. All are basic proteins, adsorbed on CM-Sephadex, with isoelectric points (pI) in the range pH 9.5–10.5. Separation of lysostaphin by isoelectric focusing in a very shallow pH gradient resolved these enzymes that have not previously been separated. The charge of each of these enzymes is similar to that on the corresponding ones from strain M18. The isoelectric point of the staphylolytic peptidase was 10.4, the pI of the amidase 9.8, and the pI of the glucosaminidase 9.5. Separation by Sephadex G-100 gel chromatography also showed the similarity in size of the corresponding enzymes from the two sources. Digestion of staphylococcal peptidoglycan with the purified staphylolytic peptidase with a pI of 10.4 and the staphylococcal endo-β-N-acetyIglucosaminidase of strain M18 gave a high recovery of disaccharide peptide monomer which was purified by Sephadex G-50 and G-25 chromatography and used as substrate for the amidases. Neither the amidase of S. aureus nor the one of lysostaphin was found to be bacteriolytic per se. The heterogeneity of the bacteriolytic activity of strain M18 was further studied by isoelectric focusing and acrylamide electrophoresis. Component A (pI 9.5) and B (pI 7) are probably isoenzymes of the endo-β-N-acetylglucosaminidase, since they had similar properties and were not separable by molecular sieve chromatography. Immunodiffusion experiments show that the glucosaminidase of S. aureus, strain M18, and the corresponding enzyme of lysostaphin are probably not structurally related which is remarkable due to the rare occurrence of bacteriolytic endo-β-N-acetylglucosaminidases in nature." @default.
- W2070507528 created "2016-06-24" @default.
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- W2070507528 date "2009-08-15" @default.
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- W2070507528 title "STUDIES ON ENDO-β-N-ACETYLGLUCOSAMINIDASE, STAPHYLOLYTIC PEPTIDASE, AND N-ACETYLMURAMYL-L-ALANINE AMIDASE IN LYSOSTAPHIN AND FROM STAPHYLOCOCCUS AUREUS" @default.
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- W2070507528 doi "https://doi.org/10.1111/j.1699-0463.1971.tb02152.x" @default.
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