Purification and some kinetic properties of rat liver ATP citrate lyase

Houston, B. and Nimmo, H.G. (1984) Purification and some kinetic properties of rat liver ATP citrate lyase. Biochemical Journal, 224(2), pp. 437-443. (doi: 10.1042/bj2240437) (PMID:6335031) (PMCID:PMC1144450)

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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.

Item Type:Articles
Glasgow Author(s) Enlighten ID:Nimmo, Professor Hugh
Authors: Houston, B., and Nimmo, H.G.
College/School:College of Medical Veterinary and Life Sciences > Institute of Molecular Cell and Systems Biology
Journal Name:Biochemical Journal
Publisher:Portland Press
ISSN (Online):1470-8728

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