Oxidative phosphorylation and adenosine triphosphatase activity in the liver mitochondria of rats administered with phenylhydrazine and hydrolyzed glucose cycloacetoacetate.

Abstract

The effect of phenylhydrazine and hydroiyzed product of glucose cycloacetoacetate (GCAh) administration on the activity of adenosine triphosphatase (ATPase) in rat-liver mitochondria has been investigated. The results are discussed in relation to the efficiency of mitochondrial oxidative phosphorylation. Phenylhydrazine was found to increase the ATPase activity both in vitro and in vivo. However, preincubation or treatment with hydrolyzed glucose cycloacetoacetate resulted in an appreciable depression of this phenylhydrazine-enhanced enzyme activity. The liver mitochondria from phenylhydrazine-administered rats showed very little difference in milligrams of total protein, but the homogenates had a high protein content as compared to the preparations from normal rats and rats administered with hydrolyzed glucose cycloacetoacetate. With citrate as the substrate, normal rat-liver mitochondria exhibited a P/O ratio of 3.0. With the same substrate, the liver mitochondria from phenylhydrazine-administered rats lowered the oxygen uptake and ATP formation, thereby resulting in a decreased P/O ratio of 2.4, whereas administration of hydrolyzed glucose cycloacetoacetate prior to phenylhydrazine resulted in a partial restoration in oxygen uptake and ATP formation, and thus yielded a P/O ratio of 2.8.