Abstract
The effect of partially purified and crude staphylococcal α-toxin (ST) on the activity of rat liver mitochondrial ATPase has been studied. The crude toxin caused marked stimulation activity of ATPase in whole mitochondria. The effect has a rapid onset and is concentration dependent. The biphasic effect upon activity of ATPase could be observed either with fresh mitochondria and partially purified ST or aged mitochondria and crude ST. Neither GTP nor ADP dephosphorylation was observed under the same conditions. PCMB completely prevented the effect of crude ST in fresh and somewhat reduced the effect in aged mitochondria. Also observed was a solubilization of ATPase which had many common enzymatic properties with crude ATPase extracted from acetone-dried mitochondria (i.e. ions requirement, substrate specificity).
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