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- W1988193754 abstract "Sonic extracts of smooth Brucella abortus, strain 19, possess two asparagine deamidases, one specifically hydrolyzing the l-isomer of asparagine and one hydrolyzing the d-isomer. l-Asparaginase is labile to repeated freezing and thawing, whereas d-asparaginase is stable to this treatment. Both enzymes appear to be sulfhydryl-type enzymes. No readily dissociable metal-ion cofactors have been found for either enzyme. d-Asparaginase is active over a wide pH range while l-asparaginase activity increases sharply at pH 8.0. The enzymes have been separated by fractional precipitation with acetic acid. Substrate saturation curves for the two enzymes are different." @default.
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- W1988193754 date "1954-03-01" @default.
- W1988193754 modified "2023-10-12" @default.
- W1988193754 title "Stereospecific asparaginases in smooth Brucella abortus, strain 19" @default.
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- W1988193754 doi "https://doi.org/10.1016/0003-9861(54)90174-5" @default.
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