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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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.
| Item Type: | Articles |
|---|---|
| Status: | Published |
| Refereed: | Yes |
| Glasgow Author(s) Enlighten ID: | Nimmo, Professor Hugh |
| Authors: | Houston, B., and Nimmo, H.G. |
| College/School: | College of Medical Veterinary and Life Sciences > School of Molecular Biosciences |
| Journal Name: | Biochemical Journal |
| Publisher: | Portland Press |
| ISSN: | 0264-6021 |
| ISSN (Online): | 1470-8728 |
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