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- W2068755710 abstract "The enzymatic properties of P2-2 enzyme were determined by using cells of M. radiodurans. The enzyme was: most active at 60°C incubation temperature, stable at 40°C in neutral buffer, and inactivated by heating at 80°C for 15min. Maximal lytic activity occurred at pH 8.5 in Tris-HCl buffer. The range of enzyme stability was between pH 5.5 and 8. Bivalent metal ions, p-chloromercuribenzoate and monoiodo acetate inhibited lytic activity. The molecular weight was estimated to be 16,000 daltons by gel filtration on Sephadex G-75. The enzymatic digestion of peptidoglycans from the cell walls of M. radiodurans and M. lysodeikticus liberated free amino groups, but neither reducing groups nor N-acetylhexosamine, indicating that the enzyme was an endopeptidase. From analysis of the N-terminal amino acids of the digests, it is suggested that the P2-2 enzyme cleaves the peptide bond at the carboxyl group of D-alanine in peptidoglycan." @default.
- W2068755710 created "2016-06-24" @default.
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- W2068755710 date "1981-01-01" @default.
- W2068755710 modified "2023-09-23" @default.
- W2068755710 title "Properties and lytic action of the P2-2 enzyme capable of lysing cells of Micrococcus radiodurans." @default.
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- W2068755710 doi "https://doi.org/10.1271/bbb1961.45.1215" @default.
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