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Difference between revisions of "Azzone 1961 J Biol Chem"

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{{Publication
{{Publication
|title=Azzone GF, Ernster L (1961) Demonstration of a requirement of high energy phosphate for the aerobic oxidation of succinate in liver mitochondria. J Biol Chem 236:1518-25.
|title=Azzone GF, Ernster L (1961) Demonstration of a requirement of high energy phosphate for the aerobic oxidation of succinate in liver mitochondria. J Biol Chem 236:1518-25.
|info=[http://www.jbc.org/content/236/5/1518.full.pdf+html PMID: 13685481 Open Access]
|info=[http://www.ncbi.nlm.nih.gov/pubmed/13685481 PMID: 13685481 Open Access]
|authors=Azzone GF, Ernster L
|authors=Azzone GF, Ernster L
|year=1961
|year=1961
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The  concept  is  developed  that  the  aerobic  oxidation  of  succinate  in  intact  liver  mitochondria  requires  an  activation  by high  energy  phosphate.  Some  implications  of  this  concept  regarding  the  enzymic  organization  of  mitochondrial  electron transport  and  oxidative  phosphorylation  are  discussed.
The  concept  is  developed  that  the  aerobic  oxidation  of  succinate  in  intact  liver  mitochondria  requires  an  activation  by high  energy  phosphate.  Some  implications  of  this  concept  regarding  the  enzymic  organization  of  mitochondrial  electron transport  and  oxidative  phosphorylation  are  discussed.
|keywords=succinate oxidation, high energy phosphate, ATP
|keywords=Succinate oxidation, High energy phosphate, ATP
}}
}}
{{Labeling
{{Labeling

Revision as of 09:57, 28 May 2015

Publications in the MiPMap
Azzone GF, Ernster L (1961) Demonstration of a requirement of high energy phosphate for the aerobic oxidation of succinate in liver mitochondria. J Biol Chem 236:1518-25.

» PMID: 13685481 Open Access

Azzone GF, Ernster L (1961) J Biol Chem

Abstract: Preincubation of rat liver mitochondria in a sucrose-KCl medium in the presence of 2 to 3 mM arsenate and 0.06 mM Dicumarol or 0.1 mM 2,4dinitrophenol for 3 to 4 minutes results in a marked depression of the succinoxidase capacity. No depression is found when the preincubation is made in the presence of Amytal, cysteine sulfinate, or inorganic phosphate. Addition of adenosine triphosphate after the preincubation stimulates succinate oxidation several-fold. The effect of adenosine triphosphate is not duplicated by cysteine sulfinate, inorganic phosphate, ethylenediaminetetraacetate, adenosine 5’-phosphate, cytidine triphosphate, uridine triphosphate, inosine triphosphate, or guanidine triphosphate. Similar results are obtained with mitochondria pretreated with dinitrophenol and adenosine 5’-phosphate.

The data are consistent with the conclusion that conditions leading to a depletion of the endogenous content of mitochondrial high energy phosphate result in a reversible depression of the succinoxidase capacity.

The concept is developed that the aerobic oxidation of succinate in intact liver mitochondria requires an activation by high energy phosphate. Some implications of this concept regarding the enzymic organization of mitochondrial electron transport and oxidative phosphorylation are discussed. ‱ Keywords: Succinate oxidation, High energy phosphate, ATP


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Organism: Rat  Tissue;cell: Liver  Preparation: Isolated mitochondria  Enzyme: Complex II;succinate dehydrogenase  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., Substrate;glucose;TCA cycle"Substrate;glucose;TCA cycle" 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, ETS"ETS" is not in the list (LEAK, ROUTINE, OXPHOS, ET) of allowed values for the "Coupling states" property. 


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