Difference between revisions of "Lam 1967 Arch Biochem Biophys"
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{{Publication | {{Publication | ||
|title=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- | |title=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. | ||
|info=[http://www.ncbi.nlm.nih.gov/pubmed/6052440 PMID: 6052440] | |info=[http://www.ncbi.nlm.nih.gov/pubmed/6052440 PMID: 6052440] | ||
|authors=Lam KW, Warshaw J, Sanadi DR | |authors=Lam KW, Warshaw J, Sanadi DR | ||
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|journal=Arch Biochem Biophys | |journal=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. | |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= | |keywords=Oxidative phosphorylation, Energy-transfer factor B, Beef heart | ||
}} | }} | ||
{{Labeling | {{Labeling | ||
|organism= | |organism=Bovines | ||
|tissues= | |tissues=Heart | ||
|preparations=Isolated | |preparations=Isolated mitochondria | ||
|enzymes=Complex II; | |enzymes=Complex II;succinate dehydrogenase, Complex V;ATP synthase | ||
|topics= | |topics=ATP | ||
|couplingstates=OXPHOS | |||
|additional=Made history | |additional=Made history | ||
}} | }} | ||
Latest revision as of 15:16, 25 November 2015
| 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
Coupling state: OXPHOS
Made history
