A FACTOR WHICH INCREASES THE DINITROPHENOL-SENSITIVITY OF THE ATP-ADP EXCHANGE REACTION OF OXIDATIVE PHOSPHORYLATION
- 1 December 1960
- journal article
- research article
- Published by Proceedings of the National Academy of Sciences in Proceedings of the National Academy of Sciences
- Vol. 46 (12), 1582-1585
- https://doi.org/10.1073/pnas.46.12.1582
Abstract
A specific, soluble protein fraction (designated M-factor) obtained from mitochondrial extracts has been found to increase the DNP-sensitivity of the ATP-ADP exchange reaction of oxidative phosphorylation in digitonin fragments of mitochondria. This factor is postulated to be either a "cementing" protein or an intermediate enzyme of the energy-coupling mechanism linking the terminal enzymatic step catalyzing the ATP-ADP exchange, which is DNP-insensitive, with a preceding, DNP-sensitive reaction. Preparations of M-factor also show C-factor activity, i.e., they promote contraction of glutathione -swollen mitochondria by ATP.Keywords
This publication has 5 references indexed in Scilit:
- RECONSTITUTION OF THE DINITROPHENOL-SENSITIVE ATP-ADP EXCHANGE REACTION OF OXIDATIVE PHOSPHORYLATIONProceedings of the National Academy of Sciences, 1960
- Studies on the mechanism of oxidative phosphorylation IV. A factor for coupled oxidation in the electron transport particleBiochimica et Biophysica Acta, 1960
- The Adenosine Triphosphate-Adenosine Diphosphate Exchange Reaction of Oxidative PhosphorylationJournal of Biological Chemistry, 1958
- Oxidative PhosphorylationScience, 1958
- A soluble protein fraction required for coupling phosphorylation to oxidation in submitochondrial fragments of beef heart mitochondriaArchives of Biochemistry and Biophysics, 1958