[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.
D000818:Animals; D001219:Aspartate Aminotransferases / Q000378:metabolism; D001224:Aspartic Acid / Q000378:metabolism; D001921:Brain / Q000378:metabolism*; D003593:Cytoplasm / Q000201:enzymology; D004195:Disease Models, Animal; D005987:Glyceraldehyde-3-Phosphate Dehydrogenases / Q000378:metabolism; D006593:Hexokinase / Q000378:metabolism; D002537:Intracranial Arteriosclerosis / Q000378:metabolism*; D007651:Keto Acids / Q000378:metabolism; D008291:Malate Dehydrogenase / Q000378:metabolism; D008293:Malates / Q000378:metabolism; D008854:Microscopy, Electron; D008928:Mitochondria / Q000201:enzymology / Q000648:ultrastructure; D010071:Oxaloacetates / Q000378:metabolism; D011817:Rabbits
D007651:Keto Acids; D008293:Malates; D010071:Oxaloacetates; D001224:Aspartic Acid; D008291:Malate Dehydrogenase; D005987:Glyceraldehyde-3-Phosphate Dehydrogenases; D001219:Aspartate Aminotransferases; D006593:Hexokinase