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. 1984 Dec 1;224(2):437–443. doi: 10.1042/bj2240437

Purification and some kinetic properties of rat liver ATP citrate lyase.

B Houston, H G Nimmo
PMCID: PMC1144450  PMID: 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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Selected References

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