Analysis of protein‐protein interactions between isoforms of malate dehydrogenase and citrate synthase

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Interaction between Citrate Synthase and Malate Dehydrogenase

The interactions between pig heart citrate synthase and mitochondrial malate dehydrogenase or cytosolic malate dehydrogenase were studied using the frontal analysis method of gel filtration and by precipitation in polyethylene glycol. This method showed that an interaction between citrate synthase and mitochondrial malate dehydrogenase occurred but no interaction between citrate synthase and cy...

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Quantitation of the interaction between citrate synthase and malate dehydrogenase.

Formation of a bienzyme complex of pig heart mitochondrial malate dehydrogenase and citrate synthase in a buffered system is demonstrated by means of a covalently attached fluorescent probe to citrate synthase. Assuming 1:1 stoichiometry of the enzymes in the complex, an apparent dissociation constant of 10(-6) M was calculated from fluorescence anisotropy measurements. The effect of various me...

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Interaction between citrate synthase and malate dehydrogenase. Substrate channeling of oxaloacetate.

The interactions between pig heart citrate synthase and mitochondrial malate dehydrogenase or cytosolic malate dehydrogenase were studied using the frontal analysis method of gel filtration and by precipitation in polyethylene glycol. This method showed that an interaction between citrate synthase and mitochondrial malate dehydrogenase occurred but no interaction between citrate synthase and cy...

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Equilibrium constants of the malate dehydrogenase, citrate synthase, citrate lyase, and acetyl coenzyme A hydrolysis reactions under physiological conditions.

The observed equilibrium constants (Kobs) of the malate dehydrogenase (EC 1.1.1.37), citrate synthase (EC 4.1.3.7) and citrate lyase (EC 4.1.3.6) reactions have been determined under near physiological conditions (38”, pH 7.0, Z = 0.25, free [Mg”+] = 10u3 M). From these values the observed standard free energy change (AGibs) for the hydrolysis of acetyl-CoA has been determined. Under the above ...

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ژورنال

عنوان ژورنال: The FASEB Journal

سال: 2019

ISSN: 0892-6638,1530-6860

DOI: 10.1096/fasebj.2019.33.1_supplement.631.37