Purification and some kinetic properties of rat liver ATP citrate lyase
Keyword(s):
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.
1979 ◽
Vol 254
(19)
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pp. 9807-9813
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1983 ◽
Vol 224
(1)
◽
pp. 299-309
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Keyword(s):
1976 ◽
Vol 251
(7)
◽
pp. 2023-2029
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1983 ◽
Vol 258
(13)
◽
pp. 8156-8162
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1986 ◽
Vol 261
(13)
◽
pp. 5936-5942
◽
1976 ◽
Vol 65
(2)
◽
pp. 375-385
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