The kinetics of rat liver citrate synthase in situ. |
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| Authors: | M A Matlib M Boesman-Finkelstein P A Srere |
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| Institution: | Basic Science Unit, Veterans Administration Hospital, and Department of Biochemistry, University of Texas Health Science Center, Dallas, Texas, U.S.A. |
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| Abstract: | The kinetics of citrate synthase in situ in toluene-treated rat liver mitochondria were studied. The Vmax, Km, and kinetic pattern for oxaloacetate were the same as those for the pure rat liver citrate synthase. The Km, for acetyl-CoA for the in situ enzyme was increased compared to pure enzyme (8.5 to 77 μm), and the sensitivity of the in situ enzyme to inhibition by ATP, NADPH, or tricarballylate was decreased. The change seen with ATP was not due to problems of small molecule diffusion. |
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