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)

Common carp (Cyprinus carpio L.), 1 kg body weight, were acclimated for 1-2 months to water temperatures of either 7-8 degrees C (cold-acclimated group) or 23-24 degrees C (warm-acclimated group). Single fast fibres and small bundles of slow fibres were isolated from the myotomal muscles and chemically skinned. Force-velocity (P-V) characteristics were determined at 7 degrees C and 23 degrees C. The contractile properties of carp muscle fibres are dependent on acclimation temperature. In the warm-acclimated group maximum isometric tensions (P0, kN m-2) are 47 +/- 6 and 64 +/- 5 for slow muscle fibres and 76 +/- 10 and 209 +/- 21 for fast muscle fibres at 7 degrees C and 23 degrees C, respectively. Maximum contraction velocities (Vmax, muscle lengths-1), are 0.4 +/- 0.05 and 1.5 +/- 0.1 at 7 degrees C (slow fibres) and 0.6 +/- 0.04 and 1.9 +/- 0.4 at 23 degrees C (fast fibres). All values represent mean +/- S.E. P0 and Vmax at 7 degrees C are around 1.5-2.0 times higher for slow and fast muscle fibres isolated from the cold-acclimated group. Fibres from 7 degrees C-acclimated carp fail to relax completely following maximal activations at 23 degrees C. The resulting Ca-insensitive force component (50-70% P0) is associated with the development of abnormal crossbridge linkages and very slow contraction velocities. Activities of enzymes associated with energy metabolism were determined at a common temperature of 15 degrees C. Marker enzymes of the electron transport system (cytochrome oxidase), citric acid cycle (citrate synthase), fatty acid metabolism (carnitine palmitoyl transferase, beta-hydroxyacyl CoA dehydrogenase) and aerobic glucose utilization (hexokinase) have 30-60% higher activities in slow muscle from cold-acclimated than from warm-acclimated fish. Activities of cytochrome oxidase and citrate synthase in fast muscle are also elevated following acclimation to low temperature. It is concluded that thermal compensation of mechanical power output by carp skeletal muscle is matched by a concomitant increase in the potential to supply aerobically-generated ATP at low temperatures.
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PMID:Force-velocity characteristics and metabolism of carp muscle fibres following temperature acclimation. 409 57

When baker's yeast spheroplasts were lysed by mild osmotic shock, practically all of the isopropylmalate isomerase and the beta-isopropylmalate dehydrogenase was released into the 30,000 x g supernatant fraction, as was the cytosol marker enzyme, glucose-6-phosphate dehydrogenase. alpha-Isopropylmalate synthase, however, was not detected in the initial supernatant, but could be progressively solubilized by homogenization, appearing more slowly than citrate synthase but faster than cytochrome oxidase. Of the total glutamate-alpha-ketoisocaproate transaminase activity, approximately 20% was in the initial soluble fraction, whereas solubilization of the remainder again required homogenization of the spheroplast lysate. Results from sucrose density gradient centrifugation of a cell-free particulate fraction and comparison with marker enzymes suggested that alpha-isopropylmalate synthase was located in the mitochondria. It thus appears that, in yeast, the first specific enzyme in the leucine biosynthetic pathway (alpha-isopropylmalate synthase) is particulate, whereas the next two enzymes in the pathway (isopropylmalate isomerase and beta-isopropylmalate dehydrogenase) are "soluble," with glutamate-alpha-ketoisocaproate transaminase activity being located in both the cytosol and particulate cell fractions.
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PMID:Subcellular localization of the leucine biosynthetic enzymes in yeast. 435 81

The contribution of muscle tissue to the increased metabolic efficiency of the obese (fa/fa) Zucker rat at 6 wk of age was examined. In vitro O2 consumption was similar in obese and nonobese soleus and extensor digitorum longus (EDL) muscles, whether the animals were fed ad libitum, fasted, or treated with triiodothyronine. No phenotypic difference in the in vitro O2 consumption was seen when the muscles were preincubated with or without exogenous insulin. Pyruvate kinase, citrate synthase, succinate dehydrogenase, and cytochrome oxidase activities were similar in the soleus and the EDL muscles of both phenotypes. Phosphofructokinase and lactate dehydrogenase activities were higher in the soleus muscles from the obese rats, whereas hexokinase activities were higher in the EDL muscles from the nonobese rats. Mitochondrial and whole muscle homogenate respiration rates were similar in both phenotypes. The soleus and EDL muscles from the obese animals weighed less than those from the nonobese, but empty carcass weights were similar. Taken together these data suggest that muscle mass, muscle O2 consumption, and muscle oxidative capacity are similar in 6-wk-old obese and nonobese rats. Therefore other tissues are probably responsible for the increased metabolic efficiency of the young obese rat.
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PMID:Oxygen consumption and oxidative capacity of muscles from young obese and nonobese Zucker rats. 609 7

The effects of nicergoline on changes in enzymatic activities induced by hypoxia and post-hypoxic recovery were studied in various brain areas of young-adult and mature Beagle dogs. In different fractions (homogenate in toto, purified mitochondria, crude synaptosomes, SM1 and SM2 synaptic mitochondria) the maximal rate (Vmax) was investigated of the more representative enzymatic activities of: a) glycolysis, b) Krebs' cycle, c) electron transfer chain, d) amino acid and acetylcholine metabolism, e) lysosomal function. The physiopathological conditions caused alterations in different enzymatic activities depending on the area and subfraction investigated. Nicergoline tended to antagonize some of these alterations. Its action was mainly on non-synaptic mitochondria by a "braking" effect on some key enzyme activities of mitochondrial metabolism (i.e. citrate synthase, cytochrome oxidase and glutamate dehydrogenase) which suggests a sparing action in the brain.
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PMID:Effect of hypoxia and pharmacological treatment on some enzyme activities in dog brain areas. 623 88

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

By a cellular subfractionation technique, synaptic and non-synaptic mitochondria from a single rat cerebral cortex were obtained. In these different mitochondrial populations the activity of citrate synthase, malate dehydrogenase, total NADH-cytochrome c reductase, cytochrome oxidase and glutamate dehydrogenase were evaluated. Except for glutamate dehydrogenase, the enzyme specific activities evaluated in the "free" mitochondrial fraction were higher than those evaluated in the "synaptic" SM1 and SM2 mitochondrial fractions, the differences between SM1 and SM2 fractions being significant. The effect of the in vivo administration of naftidrofuryl given at different doses and at different times was studied. The treatment induced few but different changes in the various mitochondrial populations.
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PMID:Synaptic and non-synaptic mitochondria from rat cerebral cortex. Characterization and effect of pharmacological treatment on some enzyme activities related to energy transduction. 661 53

The basal- and allylisopropylacetamide-induced activities of the first enzyme of heme biosynthesis, delta-aminolevulinic acid synthase (ALAS) were measured in hepatic mitochondria and cytosol of young, adult, and aged Fisher 344 rats. The total cellular ALAS activity induced by allylisopropylacetamide decreased 67% with age. The specific activity of mitochondrial ALAS in normal and induced animals decreased with aging when assayed in whole or broken mitochondria. The levels of ALAS which accumulated in the cytosol after allylisopropylacetamide administration were proportionally greater in both the young and senescent than in the mature animals. During aging, no evidence for a fragile population of mitochondria in either normal or induced animals was observed suggesting that mitochondrial matrix proteins are not released during homogenization. The hepatic mitochondrial content decreased during aging when calculated using both a membrane-bound marker enzyme cytochrome oxidase and a matrix marker enzyme citrate synthase and was unaffected by allylisopropylacetamide treatment. This reduced mitochondrial content further diminishes the level of functional ALAS available in the liver during senescence. This study confirms the age-dependent decrease in mitochondria ALAS in normal and induced animals and also suggests an age-related change in the process by which cytosolic ALAS is translocated into the mitochondria.
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PMID:Aging-related decreases in hepatic mitochondrial and cytosolic delta-aminolevulinic acid synthase during experimental porphyria. 683 17


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