A FACTOR WHICH INCREASES THE DINITROPHENOL-SENSITIVITY OF THE ATP-ADP EXCHANGE REACTION OF OXIDATIVE PHOSPHORYLATION

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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.