Cookies help us deliver our services. By using our services, you agree to our use of cookies. More information

Difference between revisions of "Penefsky 1960 J Biol Chem"

From Bioblast
(Created page with "{{Publication |title=Penefsky HS, Pullman ME, Datta A, Racker E (1960) Partial resolution of the enzymes catalyzing oxidative phosphorylation II. Participation of a soluble adeno...")
 
Line 1: Line 1:
{{Publication
{{Publication
|title=Penefsky HS, Pullman ME, Datta A, Racker E (1960) Partial resolution of the enzymes catalyzing oxidative phosphorylation II. Participation of a soluble adenosine tolphosphatase in oxidative phosphorylation. J Biol Chem 235: 3330-3336.  
|title=Penefsky HS, Pullman ME, Datta A, Racker E (1960) Partial resolution of the enzymes catalyzing oxidative phosphorylation II. Participation of a soluble adenosine triphosphatase in oxidative phosphorylation. J Biol Chem 235: 3330-3336.
|info=[http://www.jbc.org/content/235/11/3330.full.pdf+html PMID: 1373409 Open Access]
|info=[http://www.jbc.org/content/235/11/3330.full.pdf+html PMID: 1373409 Open Access]
|authors=Penefsky HS, Pullman ME, Datta A, Racker E
|authors=Penefsky HS, Pullman ME, Datta A, Racker E
|year=1960
|year=1960
|journal=J Biol Chem
|journal=J Biol Chem
|abstract=# Mechanically  fragmented  beef  heart  mitochondria  have been  resolved  by  differential  centrifugation  into  a  particulate and a  soluble  protein  component,  both  of  which  were  required  for oxidative  phosphorylation.  The  particulate  fraction  alone  catalyzed  the  oxidation  of  succinate,  β-hydroxybutyrate,  isocitrate, and  glutamate  with  little  or  no  concomitant  phosphorylation. Addition  of  the  soluble  factor  to  the  particles  resulted  in  a  net uptake  of  inorganic  phosphate  with  a  P:O  of  0.4  to  0.8.  Similarly,  both  fractions  were  required  for  a  P32-ATP  exchange.
# The  highly  purified,  soluble  coupling  factor  catalyzed  a dinitrophenol-stimulated  hydrolysis  of  ATP.
# Comparative  studies  of  the  cold  lability,  heat  stability,  and other  physical  properties  strongly  favored  the  conclusion  that the  coupling  and  ATPase  activity  were  catalyzed  by  the  same protein.
# The  significance  of  these  results  in  relation  to  current  concepts  of  the  mechanism  of  oxidative  phosphorylation  has  been discussed.
|keywords=oxidative phosphorylation, soluble ATP
}}
}}
{{Labeling
{{Labeling
|enzymes=Complex II; Succinate Dehydrogenase
|topics=Respiration; OXPHOS; ETS Capacity, ATP; ADP; AMP; PCr
|additional=Made history
|additional=Made history
}}
}}

Revision as of 19:06, 12 June 2012

Publications in the MiPMap
Penefsky HS, Pullman ME, Datta A, Racker E (1960) Partial resolution of the enzymes catalyzing oxidative phosphorylation II. Participation of a soluble adenosine triphosphatase in oxidative phosphorylation. J Biol Chem 235: 3330-3336.

» PMID: 1373409 Open Access

Penefsky HS, Pullman ME, Datta A, Racker E (1960) J Biol Chem

Abstract:

  1. Mechanically fragmented beef heart mitochondria have been resolved by differential centrifugation into a particulate and a soluble protein component, both of which were required for oxidative phosphorylation. The particulate fraction alone catalyzed the oxidation of succinate, β-hydroxybutyrate, isocitrate, and glutamate with little or no concomitant phosphorylation. Addition of the soluble factor to the particles resulted in a net uptake of inorganic phosphate with a P:O of 0.4 to 0.8. Similarly, both fractions were required for a P32-ATP exchange.
  2. The highly purified, soluble coupling factor catalyzed a dinitrophenol-stimulated hydrolysis of ATP.
  3. Comparative studies of the cold lability, heat stability, and other physical properties strongly favored the conclusion that the coupling and ATPase activity were catalyzed by the same protein.
  4. The significance of these results in relation to current concepts of the mechanism of oxidative phosphorylation has been discussed.

Keywords: oxidative phosphorylation, soluble ATP


Labels:



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.  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