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- W1591841105 abstract "Abstract β-Aspartyl peptidase from Escherichia coli has been purified 110-fold in a four-step procedure. Its molecular weight is estimated at 120,000 by gel filtration. The peptidase appears to be specific for β-aspartyl dipeptides, with maximum activity for β-l-aspartyl-l-leucine. The pH optimum is 7.5, but reactions were carried out at pH 8.0 because stability is even greater at the higher pH. The peptidase does not require metal ions for activation and is not a sulfhydryl enzyme. The apparent Km is 8.1 x 10-4 m for β-aspartylleucine." @default.
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- W1591841105 date "1968-11-01" @default.
- W1591841105 modified "2023-09-27" @default.
- W1591841105 title "Purification and Properties of a β-Aspartyl Peptidase from Escherichia coli" @default.
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- W1591841105 doi "https://doi.org/10.1016/s0021-9258(18)91928-9" @default.
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