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. |
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
Labels:
Organism: Bovines
Tissue;cell: Heart
Preparation: Isolated mitochondria
Enzyme: Complex II;succinate dehydrogenase, Complex V;ATP synthase
Regulation: ATP; ADP; AMP; PCr"ATP; ADP; AMP; PCr" is not in the list (Aerobic glycolysis, ADP, ATP, ATP production, AMP, Calcium, Coupling efficiency;uncoupling, Cyt c, Flux control, Inhibitor, ...) of allowed values for the "Respiration and regulation" property.
Coupling state: OXPHOS
Made history
