Difference between revisions of "Singer 1956 J Biol Chem"
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{{Publication | {{Publication | ||
|title=Singer TP, Kearney, EB and Bernath P (1956) Studies on succinic dehydrogenase. Isolation and properties of the dehydrogenase from beef heart. J Biol Chem 223: 599-613. | |title=Singer TP, Kearney, EB and Bernath P (1956) Studies on succinic dehydrogenase. Isolation and properties of the dehydrogenase from beef heart. J Biol Chem 223: 599-613. | ||
|info=[http://www.ncbi.nlm.nih.gov/pubmed?term=Singer%20TP%2C%20Kearney%20EB%2C%20Bernath%20P PMID: 13385208]; [http://www.jbc.org/content/223/2/599.full.pdf+html Open Access] | |info=[http://www.ncbi.nlm.nih.gov/pubmed?term=Singer%20TP%2C%20Kearney%20EB%2C%20Bernath%20P PMID: 13385208]; [http://www.jbc.org/content/223/2/599.full.pdf+html Open Access] | ||
|authors=Singer TP, Kearney, EB and Bernath P | |authors=Singer TP, Kearney, EB and Bernath P | ||
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# The QO2, has been measured as 20,000 and the turnover number as 3000 under the standard assay conditions. | # The QO2, has been measured as 20,000 and the turnover number as 3000 under the standard assay conditions. | ||
# The properties of the isolated dehydrogenase agree with those previously described for mitochondrial and other particulate preparations of the enzyme, except for properties related to the absence of contaminating hemoproteins. At 38° the pH optimum is 7.7; the K, for succinate is 1.3 X 10-3 M at 38° and 5.2 X 10-4 M at 21°. Oxalacetate, malonate, and fumarate are competitive inhibitors. Antimycin A and BAL do not inhibit the dehydrogenase. The dehydrogenase is highly sensitive to sulfhydryl reagents, p-chloromercuribenzoate inhibiting it in a reversible manner and the substrate protecting the enzyme from this type of inhibition. | # The properties of the isolated dehydrogenase agree with those previously described for mitochondrial and other particulate preparations of the enzyme, except for properties related to the absence of contaminating hemoproteins. At 38° the pH optimum is 7.7; the K, for succinate is 1.3 X 10-3 M at 38° and 5.2 X 10-4 M at 21°. Oxalacetate, malonate, and fumarate are competitive inhibitors. Antimycin A and BAL do not inhibit the dehydrogenase. The dehydrogenase is highly sensitive to sulfhydryl reagents, p-chloromercuribenzoate inhibiting it in a reversible manner and the substrate protecting the enzyme from this type of inhibition. | ||
|keywords=succinic dehydrogenase, beef heart mitochondria | |||
}} | }} | ||
{{Labeling | {{Labeling | ||
|organism=Other Mammal | |||
|tissues=Cardiac muscle | |||
|preparations=Isolated Mitochondria | |||
|enzymes=Complex II; Succinate Dehydrogenase | |||
|kinetics=Oxygen | |||
|additional=Made history | |additional=Made history | ||
}} | }} | ||
Revision as of 11:58, 11 June 2012
| Singer TP, Kearney, EB and Bernath P (1956) Studies on succinic dehydrogenase. Isolation and properties of the dehydrogenase from beef heart. J Biol Chem 223: 599-613. |
Singer TP, Kearney, EB and Bernath P (1956) J Biol Chem
Abstract:
- Succinic dehydrogenase has been isolated from beef heart mitochondria as a soluble protein in a state approaching homogeneity by physico-chemical criteria. The overall purification is about 100-fold compared with a mitochondrial acetone powder.
- The enzyme is a ferroflavoprotein cont,aining 4 atoms of ferrous (non-hemin) iron and a mole of flavin per mole of protein (200,000 gm.). The dehydrogenase may be isolated from aged starting material with 2 atoms of iron per mole and half the specific activity.
- Among the common electron acceptors, only the following function with the dehydrogenase, at the relative rates indicated in parentheses: phenazine methosulfate (100), ferricyanide (39), O2 (0.02). The first two of these acceptors react via the iron moieties, whereas O2 seems to react directly with the flavin.
- The QO2, has been measured as 20,000 and the turnover number as 3000 under the standard assay conditions.
- The properties of the isolated dehydrogenase agree with those previously described for mitochondrial and other particulate preparations of the enzyme, except for properties related to the absence of contaminating hemoproteins. At 38° the pH optimum is 7.7; the K, for succinate is 1.3 X 10-3 M at 38° and 5.2 X 10-4 M at 21°. Oxalacetate, malonate, and fumarate are competitive inhibitors. Antimycin A and BAL do not inhibit the dehydrogenase. The dehydrogenase is highly sensitive to sulfhydryl reagents, p-chloromercuribenzoate inhibiting it in a reversible manner and the substrate protecting the enzyme from this type of inhibition.
• Keywords: succinic dehydrogenase, beef heart mitochondria
Labels:
Organism: Other Mammal"Other Mammal" is not in the list (Human, Pig, Mouse, Rat, Guinea pig, Bovines, Horse, Dog, Rabbit, Cat, ...) of allowed values for the "Mammal and model" property.
Tissue;cell: Cardiac muscle"Cardiac muscle" is not in the list (Heart, Skeletal muscle, Nervous system, Liver, Kidney, Lung;gill, Islet cell;pancreas;thymus, Endothelial;epithelial;mesothelial cell, Blood cells, Fat, ...) of allowed values for the "Tissue and cell" property.
Preparation: Isolated Mitochondria"Isolated Mitochondria" is not in the list (Intact organism, Intact organ, Permeabilized cells, Permeabilized tissue, Homogenate, Isolated mitochondria, SMP, Chloroplasts, Enzyme, Oxidase;biochemical oxidation, ...) of allowed values for the "Preparation" property.
Enzyme: Complex II; Succinate Dehydrogenase"Complex II; Succinate Dehydrogenase" is not in the list (Adenine nucleotide translocase, Complex I, Complex II;succinate dehydrogenase, Complex III, Complex IV;cytochrome c oxidase, Complex V;ATP synthase, Inner mt-membrane transporter, Marker enzyme, Supercomplex, TCA cycle and matrix dehydrogenases, ...) of allowed values for the "Enzyme" property.
Made history
