Über die Hemmung der durch 2.4-Dinitro-phenol aktivierbaren Adenosintriphosphatase aus Lebermitochondrien

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Abstract
The ATPase [adenosine triphosphatase] activity of rat liver mitochondria, which is activated by 2,4-dinitrophenol, was submitted to inhibition studies. This ATPase was inhibited by succinic acid, L-malic acid and malonic acid. The inhibitory effects of the individual dicarboxylic acids were not additive. From this, it was concluded that all 3 dicarboxylic acids act at the same site and possibly inhibit one and the same enzyme. The ATPase was also sensitive to Amytal. The inhibition was additive for the individual dicarboxylic acids with Amytal. Thus Amytal and the dicarboxylic acids must have different sites of action. It is assumed that the ATPase activities, which, on one hand, are inhibited by dicarboxylic acids and, on the other hand by Amytal, correspond to different enzymes.