Protonophoric activity of NADH coenzyme Q reductase and ATP synthase in coupled submitochondrial particles from horse platelets.

Abstract

A method to prepare coupled submitochondrial particles from horse platelets is described. The method allowed us to study the protonophoric activities of both complex I and complex V following the fluorescence quenching of the monoamine 9-amino-6-chloro-2 methoxyacridine (ACMA), a probe highly sensitive to the generation of a transmembrane delta pH. We carried out a kinetic analysis of each enzyme complex studying the proton translocation and the electron transfer activities of complex I as well as the proton translocation and the ATP hydrolytic activities of complex V. A micromethod to prepare coupled submitochondrial particles from platelets might be useful to investigate cell bioenergetic damage occurring in mitochondrial diseases and ageing.

• Authors: A Baracca, L Bucchi, A Ghelli, G Lenaz
• Journal: Biochemical and biophysical research communications (Biochem Biophys Res Commun) Vol. 235 Issue 3 Pg. 469-73 (Jun 27 1997) ISSN: 0006-291X [Print] United States
• PMID: 9207178 (Publication Type: Journal Article, Research Support, Non-U.S. Gov't)

Chemical References

• Carrier Proteins
• Membrane Proteins
• NAD(P)H Dehydrogenase (Quinone)
• Adenosine Triphosphatases
• Mitochondrial Proton-Translocating ATPases
• oligomycin sensitivity-conferring protein

Topics

• Adenosine Triphosphatases (blood)
• Animals
• Blood Platelets (enzymology)
• Carrier Proteins
• Electron Transport
• Horses
• Hydrogen-Ion Concentration
• Intracellular Membranes (physiology)
• Kinetics
• Membrane Proteins (blood)
• Microchemistry
• Mitochondrial Proton-Translocating ATPases
• NAD(P)H Dehydrogenase (Quinone) (blood)
• Spectrometry, Fluorescence (methods)
• Submitochondrial Particles (enzymology)