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  • Title: Purification and some kinetic properties of rat liver ATP citrate lyase.
    Author: Houston B, Nimmo HG.
    Journal: Biochem J; 1984 Dec 01; 224(2):437-43. PubMed ID: 6335031.
    Abstract:
    A new purification procedure for rat liver ATP citrate lyase is described. The method reproducibly gives homogenous undegraded enzyme. Steady-state kinetic analysis of ATP citrate lyase was complicated by the presence of ADP, a product of the reaction, in solutions of ATP. The kinetic patterns observed were dependent on whether ADP was removed by the assay system. When assays were performed with a method in which ADP was removed, the results showed that the enzyme obeys a double-displacement mechanism with a phosphoenzyme intermediate. This resolves a controversy between the results of previous kinetic studies and those of isotope-exchange and enzyme-labelling experiments.
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