Equilibrium substrate binding studies of the malic enzyme of pigeon liver. Equivalence of nucleotide sites and anticooperativity associated with the binding of L-malate to the enzyme-manganese(II)-reduced nicotinamide adenine dinucleotide phosphate ternary complex

Malic enzyme (ME) from pigeon liver is a tetrameric protein containing apparently identical subunits. In the present study, equilibrium dialysis and fluorescence titration techniques are employed to determine the binding parameters of nucleotide cofactors, malate, and the inhibitor oxalate. ME binds...

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Veröffentlicht in:	Biochemistry (Easton) 1980-03, Vol.19 (5), p.951-962
Hauptverfasser:	Pry, Terry A, Hsu, Robert Y
Format:	Artikel
Sprache:	eng
Schlagworte:	Animals Binding Sites Columbidae Kinetics Ligands Liver - enzymology Malate Dehydrogenase - metabolism Malates Manganese - pharmacology Mathematics NADP Protein Binding
Online-Zugang:	Volltext
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