Lam 1967 Arch Biochem Biophys

Lam KW, Warshaw J, Sanadi DR (1967) The mechanism of oxidative phosphorylation XIV. Purification and properties of a second energy-transfer factor. Arch Biochem Biophys 119:477-84.

» PMID: 6052440

Lam KW, Warshaw J, Sanadi DR (1967) Arch Biochem Biophys

Abstract: A protein factor, designated as Factor B, was extracted from lyophilized acetone-washed bovine heart mitochondria and purified by ammonium sulfate fractionation, and ion-exchange chromatography on DEAE-cellulose and CM-cellulose. Centrifugation in a sucrose density gradient showed that the activity of the purified factor was closely associated with a symmetrical protein peak comprising approximately 70% of the protein. Its molecular weight was estimated to be 32,000, using hemoglobin and cytochrome c as markers. Factor B produces several-fold stimulation of ATP-driven NAD reduction, and of net phosphorylation coupled to NADH or succinate oxidation in ammonia particles. The stimulation of ATP-driven NAD reduction activity exceeds that given by an optimal amount of oligomycin, and in the presence of a saturation level of Factor B, oligomycin stimulation disappears. Also, Factor B stimulation is evident in urea-depleted particles which have been supplemented by Factor A. These particles show no stimulation by oligomycin. The results suggest that Factor B may participate in the energy transfer reactions between the respiratory chain and the terminal step resulting in ATP synthesis. • Keywords: Oxidative phosphorylation, Energy-transfer factor B, Beef heart

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Organism: Bovines  Tissue;cell: Heart  Preparation: Isolated mitochondria  Enzyme: Complex II;succinate dehydrogenase, Complex V;ATP synthase  Regulation: ATP  Coupling state: OXPHOS 

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