Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:1.9.3.1 (cytochrome oxidase)
 8,822 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Enzyme histochemical methods were performed on sporozoite infected liver tissue of rats in order to gain insight into the nutrition and metabolism of exoerythrocytic forms of Plasmodium berghei. The following enzymes were demonstrated in the hepatocytic stages of the parasites, obtained 41 and 48 h after inoculation of sporozoites: acid phosphatase, cytochrome oxidase, NADH-tetrazolium reductase, succinate dehydrogenase, NAD+ and NADP+ dependent isocitrate dehydrogenase, NADP+-dependent malate dehydrogenase, lactate dehydrogenases, 6-phosphogluconate dehydrogenase and glucose-6-phosphate dehydrogenases and alpha-glycerol-phosphate dehydrogenase. The results suggest that a conventional Embden-Meyerhoff pathway, pentose phosphate pathway and Krebs' citric acid cycle may in part be present in these exoerythrocytic parasites. Alkaline phosphatase, nucleoside polyphosphatase, 5' nucleotidase, glucose-6-phosphatase, alpha-glucan phosphorylase, NAD+ dependent malate dehydrogenase, amino-peptidase M and non-specific esterases were not detected by our techniques in the parasite. The enzyme distribution of this intrahepatocytic malaria parasite revealed by histochemistry is compared with the enzyme distribution in the other phases of the parasite's life cycle.
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PMID:Histochemical observations on the exoerythrocytic malaria parasite Plasmodium berghei in rat liver. 608 94

After long-term blockade of M-cholinoreactive structures by means of atropine activities of lactate-, malate- and isocytrate dehydrogenases (LDH, MDH, IDH, respectively) was decreased in smooth muscles of pigeon stomach. At the same time, in the sceletal muscles activities of LDH and cytoplasmic MDH was also decreased. Inhibition of adrenergic reactions as a result of reserpine administration into the birds caused a decrease of IDH activity in smooth muscles as well as of LDH, IDH and cytoplasmic MDH activities in sceletal muscles. Activity of cytochrome oxidase was unaltered in both muscle types.
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PMID:[The effect of impairment of neuroregulation on the activity of redox enzymes in the smooth muscles of the pigeon stomach]. 608 34

Changes in the maximal rate of some enzymatic activities related to energy transduction (lactate dehydrogenase; citrate synthetase and malate dehydrogenase; total NADH-cytochrome c reductase and cytochrome oxidase) and others such as glutamate dehydrogenase and acetylcholine esterase were assayed both in the purified mitochondrial fraction and in the crude synaptosomal fraction from the cerebral cortex of rats. The evaluations were performed before and after a postdecapitative normothermic ischaemia of 5, 10, 20 and 40 min duration. The ischaemic damage resulted in a decrease in the activity of mitochondrial malate dehydrogenase and total NADH-cytochrome c reductase, and of synaptosomal acetylcholine esterase. The biochemical evaluations were performed also after an intraperitoneal pretreatment with vincamine TPS, trimetazidine DC and suloctidil (50 mg/kg). These drugs induced different changes in enzyme activities as a function of the duration of ischaemia. These various interferences are discussed with regard to the possible mode of action of the drugs.
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PMID:Effect of ischaemia and pharmacological treatment on enzyme activities of cortical mitochondria and synaptosomes. 609 68

Mitochondria were isolated from whole homogenates of normal liver and Novikoff hepatomas using reorienting rate zonal centrifugation on sucrose gradients. The activities of several mitochondrial-specific enzymes and ultrastructure were compared in the two tissues. Our results indicate that cytochrome oxidase, lipoamide dehydrogenase, malate dehydrogenase, and succinate dehydrogenase activities are all higher in liver homogenates than in Novikoff hepatoma homogenates. Mitochondrial hexokinase, however, is much greater in the hepatoma than in liver. The activity of these enzymes in isolated mitochondria displayed a much different pattern. Both cytochrome oxidase and succinate dehydrogenase activities were higher in hepatoma mitochondria than in liver mitochondria. Lipoamide dehydrogenase and malate dehydrogenase, conversely, were higher in liver mitochondria. Hexokinase was found to be virtually absent in liver mitochondria but plentiful in hepatoma mitochondria. Ultrastructural studies have shown that the hepatoma mitochondria are much smaller in size, which results in a decreased rate of migration into the gradient. These studies have also shown that normal liver consists of predominantly "condensed" forms of mitochondria, whereas hepatoma contained a majority of "twisted" species. Experiments using 1% bovine serum albumin in the homogenization procedures and in the gradient have confirmed earlier observations that bovine serum albumin is essential for optimal isolation of neoplastic mitochondria.
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PMID:Characteristics of mitochondria isolated by rate zonal centrifugation from normal liver and Novikoff hepatomas. 624 94

The effect of chronic treatment (8 months) with diphenylhydantoin (DPH) on rat brain was studied. The activity of some enzymes related to energy transduction (lactate dehydrogenase, citrate synthase, and malate dehydrogenase; NADH-cytochrome c reductase and cytochrome oxidase) and neurotransmission (acetylcholine esterase) was evaluated both in the whole brain homogenate and/or in the crude mitochondrial fraction. A clear-cut decrease of acetylcholine esterase activity was observed, the decrease continuing even after treatment was discontinued. Effects on energy metabolism and on lactate dehydrogenase, malate dehydrogenase, and cytochrome oxidase are discussed.
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PMID:Acetylcholine esterase sensitivity to chronic administration of diphenylhydantoin and effects on cerebral enzymatic activities related to energy metabolism. 625 94

Changes in the maximal rate of some cerebral enzymatic activities related to 400ene transduction and neurotransmission (lactate dehydrogenase; citrate synthase and malate dehydrogenase; total NADH-cytochrome c reductase and cytochrome oxidase; glutamate dehydrogenase; acetylcholine esterase) were assayed both in the crude or purified mitochondrial fraction and in the crude synaptosomal fraction from rat whole brain or cerebral cortex. The evaluations were performed in rats before and after a postdecapitative normothermic ischemia of 5, 10, 20 and 40 min duration. Modification observed in some of these activities wer discussed for comparison with other experimental results from different researchers. At present no definite conclusions can be drawn, but certainly the observed modifications in activity of enzymes are not passive but expression of deranged metabolism of ischemic neurons.
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PMID:Brain enzymes and ischemia. 626 30

The effects of complete ischemia and of in vivo pharmacological treatment with trimetazidine were studied on some enzymatic activities related to energy transduction: lactate dehydrogenase for anaerobic glycolysis; citrate synthase and malate dehydrogenase for the Krebs' cycle; total NADH-cytochrome c reductase and cytochrome oxidase for the electron transport chain; glutamate dehydrogenase for amino acid metabolism and acetylcholine esterase for acetylcholine metabolism. These enzymatic activities were evaluated in brains of 10-day-old rats, at three different subcellular levels: homogenate in toto, purified mitochondrial fraction, crude, synaptosomal fraction. Complete normothermic post-decapitative ischemia of 30 min duration increased the activity of cytochrome oxidase in the homogenate in toto and increased the activities of citrate synthase and malate dehydrogenase in the purified mitochondrial fraction, the activities of the enzymes evaluated in the crude synaptosomal fraction being unaffected. The i.p. treatment with trimetazidine (at the dose level of 50 mg . kg-1) was without any significant effect on the tested enzymatic activities.
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PMID:Effects of ischemia and pharmacological treatment on subcellular fractions from neonatal rat brain. 628 22

In order to investigate the in vivo pharmacological effects of the drug naftidrofuryl, we prepared populations of synaptic and nonsynaptic mitochondria from rat brain cortex. In these different mitochondrial populations the activities of citrate synthase, malate dehydrogenase, total NADH cytochrome c reductase, cytochrome oxidase, and glutamate dehydrogenase were evaluated. Except for glutamate dehydrogenase, the specific activities of the enzymes evaluated in the "free" mitochondrial fraction were higher than those observed in the "synaptic" SM1 and SM2 mitochondrial fractions, the difference between SM1 and SM2 fractions being significant. The in vivo administration of naftidrofuryl induced few and different changes in the various mitochondrial populations.
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PMID:Rat cortex synaptic and nonsynaptic mitochondria: enzymatic characterization and pharmacological effects of naftidrofuryl. 631 51

relationship between levels of cAMP and catabolite repression in yeasts has been investigated. Strains of Saccharomyces cerevisiae, Schizosaccharomyces pombe and Kluyveromyces fragilis were used. The yeasts were grown on different carbon sources to attain various degrees of repression. Galactose repressed as much as glucose, while maltose was less effective. Full derepression was achieved with ethanol. The enzymes tested were fructose-bisphosphatase, malate dehydrogenase, glutamate dehydrogenase (NAD dependent), cytochrome oxidase and isocitrate lyase (this last enzyme was found to be absent in Schizosaccharomyces). The levels of cAMP were 2-3 times higher in the repressed conditions than in the derepressed ones. It is therefore concluded that in yeasts catabolite repression is not mediated by a lowering of the intracellular concentration of cAMP.
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PMID:Catabolite repression in yeasts is not associated with low levels of cAMP. 632 8

We have determined the subcellular localization of an endopeptidase activity able to degrade gonadotropin releasing hormone (GnRH) and present in the rat adenohypophysis. After fractionation of tissue homogenates in 0.25 M sucrose by differential centrifugation, about 25% of the total cellular GnRH degrading activity was found to be sedimentable and recovered from heavy (M) and light (L) mitochondrial fractions with a distribution pattern similar to that of the mitochondrial and lysosomal reference enzymes cytochrome oxidase and beta-galactosidase. Upon further fractionation on sucrose density gradients, the activity comigrated with mitochondria. The peptidase appears endowed with a structure-linked latency; the activity is low in a freshly prepared mitochondrial fraction and increases upon treatment with membrane disrupting agents in a manner similar to that of malate dehydrogenase, a component of the mitochondrial matrix. Determination of GnRH cleavage sites was performed by amino acid analysis of the fragments obtained after incubation of the peptidase with (3H)-GnRH labelled on the pyroglutamic acid residue, in presence of carboxypeptidase and peptidyldipeptidase inhibitors. The fragments were separated by ion-exchange chromatography on an Aminex Q-15S column and purified by chromatography on silica gel plates. Fragments 1-2, 1-3, 1-4, 1-5 and 1-6 were all present as early as 1 min after the beginning of incubation. Formation of each of them was inhibited to the same extent by EDTA, mersalyl acid, dithioerythritol and Na deoxycholate. The same fragmentation pattern was observed after partial purification of the enzyme by gel filtration. These data indicate that cleavage of several peptide bonds may result from a possibly single endopeptidase located in the mitochondrial matrix space.
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PMID:Characterization of a neutral endopeptidase localized in the mitochondrial matrix of rat anterior pituitary tissue with GnRH as a substrate. 637 12


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