Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:1.4.1.2 (glutamate dehydrogenase)
 4,380 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Treatment of rat liver mitochondria with digitonin followed by differential centrifugation was used to resolve the intramitochondrial localization of both soluble and particulate enzymes. Rat liver mitochondria were separated into three fractions: inner membrane plus matrix, outer membrane, and a soluble fraction containing enzymes localized between the membranes plus some solublized outer membrane. Monoamine oxidase, kynurenine hydroxylase, and rotenone-insensitive NADH-cytochrome c reductase were found primarily in the outer membrane fraction. Succinate-cytochrome c reductase, succinate dehydrogenase, cytochrome oxidase, beta-hydroxybutyrate dehydrogenase, alpha-ketoglutarate dehydrogenase, lipoamide dehydrogenase, NAD- and NADH-isocitrate dehydrogenase, glutamate dehydrogenase, aspartate aminotransferase, and ornithine transcarbamoylase were found in the inner membrane-matrix fraction. Nucleoside diphosphokinase was found in both the outer membrane and soluble fractions; this suggests a dual localization. Adenylate kinase was found entirely in the soluble fraction and was released at a lower digitonin concentration than was the outer membrane; this suggests that this enzyme is localized between the two membranes. The inner membrane-matrix fraction was separated into inner membrane and matrix by treatment with the nonionic detergent Lubrol, and this separation was used as a basis for calculating the relative protein content of the mitochondrial components. The inner membrane-matrix fraction retained a high degree of morphological and biochemical integrity and exhibited a high respiratory rate and respiratory control when assayed in a sucrose-mannitol medium containing EDTA.
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PMID:Enzymatic properties of the inner and outer membranes of rat liver mitochondria. 569 70

2-Isopropyl-6-methyl-4-S-pyrimidinyl diethyl thiophosphate (isodiazinon) has been synthesized by an unambiguous route. Rats treated with isodiazinon over a 100-day period show decreased levels of liver ferrochelatase. Rats treated with diazinon and isodiazinon in combination over the same period show a more marked decrease in liver ferrochelatase activity as well as a decrease in the activity of coproporphyrinogen oxidase. Treatment of rats with stabilised diazinon over the same period is not associated with a decrease in the activity of either enzyme. Neither diazinon nor isodiazinon causes a decrease in the activity of glutamate dehydrogenase, succinate dehydrogenase or kynurenine hydroxylase, suggesting that the effect is specific to the porphyrin biosynthesis pathway and not due to mitochondrial damage.
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PMID:The site of inhibition of porphyrin biosynthesis by an isomer of diazinon in rats. 662 36