[Generation and transport systems of restored equivalents in rabbit brain tissue under experimental atherosclerosis]

Distrubances are found in the shuttle transport systems of extramitochonidral hydrogen in the brain of rabbits with experimental atherosclerosis, the catalytical function of glyceraldehyde phosphate dehydrohenase being preserved. A decrease in the activity of cytoplasmatic glycerophosphate dehydrogenase was observed parallel with an increase in the content of glycerophosphate. Deviations from the norm in the malate-aspartate shunt are pronounced in a considerable activation of mitochondrial malate dehydrogenase, inhibition of aspartate amino transpherase, accumulation of oxaloacetate and exhaustion of the malate stock. Beta-Oxybutyrate dehydrogenase activates sharply, the content of acetoacetate increases. The total activity of hexoxokinase in cytoplasm and mitochondria remains practically unchanged.