Difference between revisions of "Racker 1967 J Biol Chem"
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{{Publication | {{Publication | ||
|title=Racker E, Horstman LL (1967) Partial resolution of the enzymes catalyzing oxidative phosphorylation XIII. Structure and function of submitochondrial particles completely resolved with respect to coupling factor 1. J Biol Chem 242: 2547-2551. | |title=Racker E, Horstman LL (1967) Partial resolution of the enzymes catalyzing oxidative phosphorylation XIII. Structure and function of submitochondrial particles completely resolved with respect to coupling factor 1. J Biol Chem 242: 2547-2551. | ||
|info=[http://www.jbc.org/content/242/10/2552.full.pdf+html PMID: 4290709] | |info=[http://www.jbc.org/content/242/10/2552.full.pdf+html PMID: 4290709 Open Access] | ||
|authors=Racker E, Horstman LL | |authors=Racker E, Horstman LL | ||
|year=1967 | |year=1967 | ||
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# Submitochondrial beef heart particles devoid of endogenous ATPase could bind the purified yeast enzyme without changing its immunological specificity. The ATPase activity of the resultant "hybrid" particles, like that of beef heart particles, was strongly inhibited by low levels of rutamycin. In contrast, submitochondrial particles from yeast were much less sensitive to this inhibitor. | # Submitochondrial beef heart particles devoid of endogenous ATPase could bind the purified yeast enzyme without changing its immunological specificity. The ATPase activity of the resultant "hybrid" particles, like that of beef heart particles, was strongly inhibited by low levels of rutamycin. In contrast, submitochondrial particles from yeast were much less sensitive to this inhibitor. | ||
# The yeast enzyme stimulated oxidative phosphorylation in beef heart particles which were deficient in, but not devoid of, endogenous ATPase. The stimulation was dependent on the presence of beef heart coupling factor 1 (F1) in these particles and was unaffected by the antiserum against the yeast enzyme. Antiserum against beef heart F1 strongly inhibited phosphorylation. These results suggest that yeast F1, in contrast to beef heart F1, does not significantly participate in phosphate transfer reactions when it functions as a coupling factor in beef heart particles. Rather, it is proposed that the stimulation by yeast F1 is due to an effect on the membrane structure. | # The yeast enzyme stimulated oxidative phosphorylation in beef heart particles which were deficient in, but not devoid of, endogenous ATPase. The stimulation was dependent on the presence of beef heart coupling factor 1 (F1) in these particles and was unaffected by the antiserum against the yeast enzyme. Antiserum against beef heart F1 strongly inhibited phosphorylation. These results suggest that yeast F1, in contrast to beef heart F1, does not significantly participate in phosphate transfer reactions when it functions as a coupling factor in beef heart particles. Rather, it is proposed that the stimulation by yeast F1 is due to an effect on the membrane structure. | ||
|keywords=oxidative phosphorylation, submitochondrial particles, coupling factor 1 | |keywords=oxidative phosphorylation, submitochondrial particles, coupling factor 1 | ||
}} | }} | ||
Revision as of 16:20, 20 June 2012
| Racker E, Horstman LL (1967) Partial resolution of the enzymes catalyzing oxidative phosphorylation XIII. Structure and function of submitochondrial particles completely resolved with respect to coupling factor 1. J Biol Chem 242: 2547-2551. |
Racker E, Horstman LL (1967) J Biol Chem
Abstract:
- A Mg++-dependent adenosine triphosphatase was solubilized and purified from bakers' yeast mitochondria. The enzyme resembled mitochondrial ATPase from beef heart with respect to substrate specificity, cold lability, and other physical properties.
- An antiserum against the purified yeast enzyme inhibited the ATPase activity of the soluble enzyme as well as ATPase and oxidative phosphorylation in submitochondrial yeast particles. Mitochondrial ATPase from beef heart or from Neurospora crassa was not inhibited by the antiserum.
- Submitochondrial beef heart particles devoid of endogenous ATPase could bind the purified yeast enzyme without changing its immunological specificity. The ATPase activity of the resultant "hybrid" particles, like that of beef heart particles, was strongly inhibited by low levels of rutamycin. In contrast, submitochondrial particles from yeast were much less sensitive to this inhibitor.
- The yeast enzyme stimulated oxidative phosphorylation in beef heart particles which were deficient in, but not devoid of, endogenous ATPase. The stimulation was dependent on the presence of beef heart coupling factor 1 (F1) in these particles and was unaffected by the antiserum against the yeast enzyme. Antiserum against beef heart F1 strongly inhibited phosphorylation. These results suggest that yeast F1, in contrast to beef heart F1, does not significantly participate in phosphate transfer reactions when it functions as a coupling factor in beef heart particles. Rather, it is proposed that the stimulation by yeast F1 is due to an effect on the membrane structure.
• Keywords: oxidative phosphorylation, submitochondrial particles, coupling factor 1
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., Yeast; Fungi"Yeast; Fungi" 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.
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 Enzyme: Complex V; ATP Synthase"Complex V; ATP Synthase" 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., Marker Enzyme"Marker Enzyme" 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. Regulation: Respiration; OXPHOS; ETS Capacity"Respiration; OXPHOS; ETS Capacity" 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., 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.
Made history
