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Subunit equilibria of porcine heart citrate synthase. Effects of enzyme concentration, pH, and substrates. by A J McEvily; J H Harrison is a Biochemistry, Genetics and Molecular Biology article available to read on EtoBox.

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Porcine heart citrate synthase, a dimeric protein of M, = 100,000 composed of two identical subunits, is shown to undergo a monomer-dimer equilibrium. The extent of dimerization is found to be dependent on the concentration of citrate synthase, pH, ionic strength, and the specific buffer system employed. Oxaloacetate and citrate, substrates for the forward and reverse reaction catalyzed by citrate synthase, affect dimerization at concentrations of the protein which exists as monomer in their absence. The dissociation of citrate synthase dimers has been demonstrated utilizing the techniques of gel permeation chromatography, fluorescence polarization, fluorescence energy transfer, and heat denaturation. Earlier studies of citrate synthase quarternary structure found the protein to be nondissociable except under denaturing conditions or extensive modification; however, most former studies were performed at relatively high protein concentration, ionic strength, and pH, conditions which stabilize the dimer. In light of recent evidence derived from x-ray crystallographic studies showing amino acid residues from one subunit contributing to the citrate and CoA binding sites of the other, t

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Author

A J McEvily; J H Harrison

Publisher

Elsevier BV

Published

1986

Language

EN

Field

Biochemistry, Genetics and Molecular Biology (Life Sciences)