Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts: Gene/Protein Disease Symptom Drug Enzyme Compound   Target Concepts: Gene/Protein Disease Symptom Drug Enzyme Compound

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Query: EC:1.3.5.1 (succinate dehydrogenase)
8,177 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Metabolic activity of rat lungs were studied in normal state and in acute hypoxia, caused by an effect of rarefied atmosphere (3 hrs, "height" 10,000 m). Glycolytic splitting of carbohydrates and catabolism of proteins were increased in lungs under hypoxic stress. In hypoxia activities of adlobase, pyruvate kinase, succinate dehydrogenase, 5-hydroxytryptophan decarboxylase were increased, but hexokinase activity was decreased. Activities of lipase, lactate dehydrogenase and NAD-dependent malate dehydrogenase were not altered, whereas the ratio in specific activity of cytoplasmic malate dehydrogenase and lactate dehydrogenase was decreased.
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PMID:[Effect of acute hypoxia on the metabolic activity of lung tissue]. 70 55

The activities of twelve enzymes were measured in crude extracts from cells of Escherichia coli K-10 grown aerobically or anaerobically in a defined medium in the presence or absence of nitrate. The activities of isocitrate dehydrogenase, aconitate hydratase, 2-oxoglutarate dehydrogenase, malate dehydrogenase, malic enzyme, and D-lactate dehydrogenase (NAD+-independent) were found to be higher in cells grown in nitrate respiration than in those in fermentation, but lower than in those in respiration. This finding may explain the incomplete oxidation in nitrate respiration and, on the other hand, suggests the operation of the tricarboxylic acid even under these conditions. The activities of succinate dehydrogenase and alcohol dehydrogenase in relation to the formation of fermentation product were as high in cells grown in fermentation as in those in respiration and were low in those in nitrate respiration. However, that ratio of the activities in the latter case to the activities in respiration was the same as the ratio for most enzymes in the tricarboxylic acid cycle. The level of lactate dehydrogenase (NAD+-dependent) was not affected by nitrate respiration but its activity in the extract was inhibited by nitrate and nitrite. The absence of lactate in the anaerobic culture with nitrate may be due to this inhibition as well as NADH oxidation by nitrate. Levels of glucose-6-phosphate dehydrogenase and glutamate dehydrogenase were not altered by the growth conditions and that of pyruvate dehydrogenase was low only in cells grown in fermentation.
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PMID:Effect of nitrate reduction on the enzyme levels in carbon metabolism in Escherichia coli. 77 52

Tetrahymena pyriformis ST (3 X 10-4 cells/ml) was treated with 0.1 mg/ml chloramphenicol (CAP). Cell division ceased after 1.5 divisions with no decreased viability. Total mitochondrial volume and succinic dehydrogenase (SDH) activity/liter increased 1.7-fold and 3-fold, respectively. SDH activity/cell decreased whereas malate dehydrogenase activity/cell and respiratory control ratios and P:O ratios of isolated mitochondria were unchanged in treated cells. During 12 hours of growth in CAP the total surface area of mitochondrial inner and outer membrane was essentially unchanged or increased 4-fold, respectively. Mitochondria from cells treated with chloramphenicol had decreased size, buoyant density and protein:lipid ratio in the membranes. The membrane ubiquinone:protein ratio was unchanged. Tetrahymena cells contained 3.6 X 10-minus 12 g of mitochondrial DNA and 6,800 mitochondria in a volume of 41,000 mu-3. A 4-hour treatment with CAP caused a 4-fold increase in the number of mitochondria/cell and a 10-fold increase in mitochondria/liter in contrast to a 4-fold increase in number of mitochondria/liter in control cells. Thus CAP stimulated division of mitochondria. Individual mitochondria of treated cells had one-tenth the volume of control mitochondria. The rate of increase of mitochondrial DNA/liter was the same in control and CAP-treated cultures. The amount of DNA/mitochondrion decreased 75% in CAP-treated cells due to the rapid division of mitochondria. The cell volume, cell protein content and mitochondrial DNA content/cell decreased with growth of control cultures.
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PMID:Effect of chloramphenicol on replication of mitochondria in Tetrahymena. 80 71

The regulation of alpha-ketogluterate dehydrogenase, succinate dehydrogenase, fumarase, malate dehydrogenase, and malic enzyme has been studied in Bacillus subitilis. The levels of these enzymes increase rapidly during late exponential phase in a complex medium and are maximal 1 to 2 h after the onset of sporulation. Regulation of enzyme synthesis has been studied in the wild type and different citric acid cycle mutants by adding various metabolites to the growth medium. Alpha-ketoglutarate dehydrogenase is induced by glutamate or alpha-ketoglutarate; succinate dehydrogenase is repressed by malate; and fumarase and malic enzyme are induced by fumarate and malate, respectively. The addition of glucose leads to repression of the citric acid cycle enzymes whereas the level of malic enzyme is unaffected. Studies on the control of enzyme activities in vitro have shown that alpha-ketoglutarate dehydrogenase and succinate dehydrogenase are inhibited by oxalacetate. Enzyme activities are also influenced by the energy level, expressed as the energy charge of the adenylate pool. Isocitrate dehydrogenase, alpha-ketoglutarate dehydrogenase, succinate dehydrogenase, and malic enzyme are inhibited at high energy charge values, whereas malate dehydrogenase is inhibited at low energy charge. A survey of the regulation of the citric acid cycle in B.subtilis, based on the present work and previously reported results, is presented and discussed.
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PMID:Regulation of the dicarboxylic acid part of the citric acid cycle in Bacillus subtilis. 80 68

The myoepithelium of developing, lactating, and involuting mammary gland of the mouse exhibits a high alkaline phosphatase activity. The content of the alveoli and the apical plasma membrane of gland cells histochemically show enzyme activity before and after lactation but not during milk secretion. In the course of involution the alveoli shrink in size and the reaction of alkaline phosphatase becomes stronger in the gland tissue. In whole breast tissue the enzyme activity decreases, because in this time a great part of the alveoli are degraded and replaced by connective tissue and fat. As measured by a scanning microdensitometer the activity of some oxydoreductases (3-hydroxybutyrate dehydrogenase, lactate dehydrogenase, malate dehydrogenase, and succinate dehydrogenase) increase in proceeding development of the mammary gland and reach their highest level at the time of lactation. Already 12 h after the start of involution the oxydoreductases loose 30 to 50% of their activity and undergo a further reduction 3 to 4 days later. On the other side the activity of lysosomal enzymes increase during involution. beta-Glucuronidase and leucine aminopeptidase have their highest activity in the early stage of involution, whereas acid phosphatase predominate in the late period of gland degradation.
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PMID:[Microdensitometric measurement enzyme activities in the mammary gland of the mouse]. 83 21

In the presented study the influence of freezing and freeze-drying on enzyme activity is described. Attention is paid to 16 enzymes which can be used for quantitative enzyme histochemical techniques. With the exception of succinate dehydrogenase only, no significant inactivation during freezing and freeze-drying procedures could be demonstrated with lactate dehydrogenase, malate dehydrogenase (NAD+), malate dehydrogenase (decarboxylating) (NADP+), isocitrate dehydrogenase (NADP+), glucose-6-phosphate dehydrogenase, 6-phosphogluconate dehydrogenase, NADH-oxydoreductase, mitochondrial glycerol-3-phosphate dehydrogenase, cytochrome c oxidase, phosphoglucomutase, glucosephosphate isomerase, glucose-6-phosphatase, acid phosphatase, beta-glucuronidase and non specific aryl esterase. Therefore, the results supply a sound foundation for those quantitative enzyme histochemical techniques in which tissue specimens are frozen or frozen-dried before enzyme estimations are performed.
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PMID:The influence of freezing and freeze-drying of tissue specimens on enzyme activity. 87 Apr 61

Muscle samples from the vastus lateralis and maximal oxygen uptakes were obtained from 22 male and 7 female competitive cyclists. 19 untrained males, and 10 untrained females. Eleven of the 22 male cyclists were designated elite cyclists (Group A) on the basis of their success in national and/or international competition. The remaining 11 male cyclists (Group B) were also trained but had not achieved the same level of competitive success. Significant mean differences (P less than 0.05) between Groups A and B were found for VO2 max (67 and 57 ml/kg/min), malate dehydrogenase (MDH) and phosphorylase (PH), in biopsied muscle. No differences were evident between Groups A and B for % slow twitch (ST) and % fast twitch (FT) fibers, or in area FT or ST. Nor was there any difference in the mean activities of succinate dehydrogenase (SDH) and lactate dehydrogenase (LDH) between the groups. Significant correlations were found between VO2 max and SDH, VO2 max and MDH, and between SDH and MDH. These data also indicate that an extremely high percentage of FT or ST fibers may not be a requirement for success in competitive cycling as has been found in earlier studies on sprint or endurance running.
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PMID:Characteristics of skeletal muscle in competitive cyclists. 89 26

The effects of 8 weeks' endurance training on muscle metabolism at rest and after a submaximal bicycle ergometer exercise were studied in 31 previously sedentary men, aged 56-70. Training consisted of 3-5 one hour exercise bouts per week including walking-jogging, swimming, gymnastics and ball games. The effects of training were similar to those previously reported for younger men. Mean maximal oxygen uptake increased (11%), as did the resting values for muscle glycogen concentration, the enzymes representing aerobic energy metabolism (malate dehydrogenase, succinate dehydrogenase), and also some of the anaerobic enzymes (creatine phosphokinase, lactate dehydrogenase). Lactate production during submaximal work decreased. The enzyme activities were lower following acute exercise both before and after training.
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PMID:Effects of 8 weeks' endurance training on skeletal muscle metabolism in 56-70-year-old sedentary men. 91 82

The state-3 rate of respiration of potato tuber mitochondria is inhibited by concentrations of KCl or NaCl above 125 mM, and by concentrations of sucrose, lactose, or maltose above 500 mM, but not at all by mannitol, glucose, glycine, or proline up to a concentration of 1500 mM in the medium. Mitochondria from cauliflower, beetroot, cucumber, rock melon, and watermelon behave very similarly to those from potato tuber. The variable response to different solutes proves that the reduction in respiration is not a simple function of the chemical potential of water in the medium. Disruption of potato mitochondria by ultrasonic vibration does not relieve the inhibition of succinate oxidation caused by KCl or sucrose. However, treatment with detergent abolishes completely the inhibition of respiration by sucrose. Inhibition of succinate dehydrogenase [Succinate:PMS, oxidoreductase (EC.1.3.99.1)] and malate dehydrogenase [L-Malate:NAD oxidoreductase (EC.1.1.1.37)] activities by sucrose is less than the inhibition of succinate- and malate-dependent oxygen uptake by the potato mitochondria. Limited substrate uptake and, alternatively, reduced electron flow as a consequence of a direct effect of solute on the mitochondrial membrane are considered as possible mechanisms of inhibition.
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PMID:The response of plant mitochondria to media of high solute content. 97 40

Histologic investigations together with histochemical and photometric measurements of enzyme activities were performed in retina of rabbits, whose blood supply had been totally interrupted for 1h. A retinal edema developed affecting the internal layers between the inner limiting membrane and the internal plexiform and ganglion cell layer. Although this edema was quite remarkable at the posterior pole of the eye, it diminished toward the periphery, disappearing near the ora serrata. The activities of the following enzymes were investigated: hexokinase, glucose 6-phosphate dehydrogenase, aldolase, glyceraldehydephosphate dehydrogenase, lactate dehydrogenase, malate dehydrogenase, succinate dehydrogenase, ATPase, and phosphorylase. The most striking finding was the total disappearance of phosphorylase activity under pressure ischemia. ATPase and aldolase showed a decreased activity in the ischemic retina, and malate dehydrogenase a slightly diminished one. Concerning the other enzymes, no significant differences between normal and ischemic retina were observed.
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PMID:Enzymologic and histologic investigations in normal and pressure-ischemic retina of rabbits. 108 79


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