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- W936712898 abstract "Publisher Summary The chapter describes the preparation of citrate lyase from Klebsiella aerogenes (Aerobacter aerogenes). The purified enzyme is activated by a range of divalent metal ions (Mg++, Mn++, Fe++, and Zn++), shows optimal activity at pH 8.0-9.0, and is powerfully inhibited by oxaloacetate. The keto form of this compound is a substrate for the enzyme, but the enol form is not and may be responsible for the inhibition observed. The spectrophotometric assay of citrate lyase is based on measurement of oxaloacetate accumulation. The method has been modified by using triethanolamine-hydrochloric acid buffer which does not form complexes with magnesium. Klebsiella aerogenes, NCIB 418 (British), are grown without aeration at 37° in 10 liter flasks filled to the neck with medium of the following composition: 9 trisodium citrate.2H2O; 2KH2PO4; 1(NH4)2SO4; 0.4 MgSO4.7H20; and adjusted to pH 7.0 with sodium hydroxide. The cells may alternatively be disrupted by sonic vibration." @default.
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- W936712898 date "1969-01-01" @default.
- W936712898 modified "2023-09-24" @default.
- W936712898 title "[28] Citrate lyase" @default.
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- W936712898 doi "https://doi.org/10.1016/0076-6879(69)13033-5" @default.
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