Characterization of shuttle mechanisms for the transport of reducing equivalents into mitochondria.

  title={Characterization of shuttle mechanisms for the transport of reducing equivalents into mitochondria.},
  author={Arthur I. Cederbaum and Charles S. Lieber and Diana S. Beattie and Emanuel Rubin},
  journal={Archives of biochemistry and biophysics},
  volume={158 2},

Magnitude of malate-aspartate reduced nicotinamide adenine dinucleotide shuttle activity in intact respiring tumor cells.

Measurements of respiration, CO2 and lactate production, and changes in the levels of various key metabolites of the glycolytic sequence and tricarboxylic acid cycle were made on five lines of rodent ascites tumor cells, indicating that on the average about one-third of the respiratory adenosine triphosphate is generated by electron flow originating from cytosolic NADH via the malate-aspartate shuttle.

Fatty Acid Oxidation , Substrate Shuttles , and Activity of the Citric Acid Cycle in Hepatocellular Carcinomas of Varying Differentiation 1

A study was made of fatty acid oxidation, oxygen consumption, and citric acid cycle activ ity by mitochondria from tumor H-252 to determine the mechanism responsible for the low activity of the fatty acid shuttle.

Influence of the Malate‐Aspartate Shuttle on Oxidative Metabolism in Synaptosomes

Abstract: β‐Methyleneaspartate, a specific inhibitor of aspartate aminotransferase (EC, was used to investigate the role of the malate‐aspartate shuttle in rat brain synaptosomes.



The compartmentation of CoA and fatty acid activating enzymes in rat liver mitochondria.

It is concluded that fatty acid oxidation in mitochondria can be explained by a simple two compartment model where the inner membrane is the permeability barrier and atractyloside is unsuitable for the study of the compartmentation of fatty acid activating enzymes in mitochondia.

The permeability of mitochondria to oxaloacetate and malate.

The results are discussed in relation to the hypothesis that malate acts as a carrier of reducing equivalents between mitochondria and cytoplasm, indicating the presence in the mitochondria of an energy-independent transhydrogenase system.

Inhibition of gluconeogenesis by butylmalonate in perfused rat liver.