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)

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

Cells of the aerotolerant anaerobe Giardia lamblia respire in the presence of oxygen. Endogenous respiration is stimulated by glucose but not by other carbohydrates and Krebs cycle intermediates. Endogenous and glucose-stimulated respiration are insensitive to cyanide, malonate, and 2,4-dinitrophenol, but are inhibited by atabrin and iodoacetamide. G. lamblia produces ethanol, acetate and CO2 both aerobically and anaerobically either from endogenous reserves or exogenous glucose. Molecular hydrogen is not produced. The following enzyme activities were detected in homogenates: hexokinase, fructose-biphosphate aldolase, pyruvate kinase, phosphoenolpyruvate carboxykinase, malate dehydrogenase, malate dehydrogenase (decarboxylating), pyruvate synthase, acetyl-CoA synthetase, alcohol dehydrogenase (NADP+), NADH dehydrogenase, NADPH dehydrogenase, NADPH oxidoreductase and superoxide dismutase. The enzymes of energy and carbohydrate metabolism are nonsedimentable (109 000 x g for 30 min). Activities of lactate dehydrogenase, hydrogenase, phosphate acetyltransferase, acetate kinase, citrate synthase, succinate dehydrogenase, fumarate hydratase and catalase were below the limits of detection. The results suggest the occurrence of glycolysis, energy production by substrate level phosphorylation and a flavin, iron-sulfur protein mediated electron transport system as well as the absence of cytochrome mediated oxidative phosphorylation and functional Krebs cycle.
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PMID:Energy metabolism of the anaerobic protozoon Giardia lamblia. 610 7

The ability of phenazine methosulphate to transfer electrons from reduced coenzymes to a tetrazolium salt, neotetrazolium chloride, after exposure to light for various periods of time has been studied. Enzymes assayed for this purpose were: glucose-6-phosphate dehydrogenase been studied. Enzymes assayed for this purpose were: glucose-6-phosphate dehydrogenase (NADP+-dependent); lactate dehydrogenase (NAD+-dependent) and succinate dehydrogenase (flavoprotein-dependent). Enzyme activity was measured in sections of rodent liver by scanning and integrating microdensitometry. Phenazine methosulphate in solution was found to be sufficiently stable in light for up to two hours for reproducible quantitative measurements of cytochemical dehydrogenase activity to be obtained over this period.
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PMID:The sensitivity to light of solutions of phenazine methosulphate: a quantitative cytochemical study. 618 Oct 23

When strain C3 of Klebsiella pneumoniae is grown on a minimal medium with excess glucose, isocitrate dehydrogenase, malate dehydrogenase, and succinate dehydrogenase specific activities increase in the last period of the exponential growth phase and in the beginning of the stationary phase. Glucose exhaustion does not alter the development of malate dehydrogenase and succinate dehydrogenase, but specific activities are higher than those obtained with excess glucose. In contrast, glucose exhaustion can be correlated with a decrease of isocitrate dehydrogenase specific activity in the stationary phase. Induction of strain C3 isocitrate dehydrogenase by glucose in complex medium and repression by cAMP in mineral medium were observed. Glucose induction and the NADP/NADPH ratio are suggested as regulatory mechanisms controlling isocitrate dehydrogenase synthesis in the Enterobacteriaceae, but the former appears to be restricted to some Klebsiella strains.
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PMID:Effect of the carbon source and cyclic AMP on isocitrate dehydrogenase, succinate dehydrogenase, and malate dehydrogenase in Klebsiella pneumoniae C3. 629 82

The peritoneal macrophages of mice treated with lysozyme were studied by cytochemical assay. In single and repeated doses of 0.5-5 mg/kg lysozyme induced an increase in macrophage metabolism. This was evident from an increased activity of succinate dehydrogenase, NADP X N-DH and the enzymes catalyzing glycolysis typical of these cells (lactate dehydrogenase and alpha-glycerophosphate). The changes in the activity of the enzymatic systems were most pronounced in minute and less mature macrophages after repeated administrations of the drugs. In a dose of 50 mg/kg lysozyme somewhat decreased the activity of a number of the enzymes. In the doses optimal for the macrophage activity lysozyme had a low effect on the infection resistance and slightly increased the cephotaxim efficiency in experimental staphylococcal infection. This may be mainly due to the immunomodulating effect of lysozyme and its low effect on the large macrophages having the bactericidal effect.
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PMID:[Experimental effect of lysozyme on macrophage metabolism and resistance to infection]. 633 Dec 92

The effects of gossypol, a polyphenolic compound isolated from the cotton plant upon six oxidoreductases from cultured epimastigotes of Typanosoma cruzi were studied. Gossypol was a powerful inhibitor of the alpha-hydroxyacid and malate dehydrogenases, NAD-linked enzymes, and of glutamate dehydrogenase, malic enzyme and glucose-6-phosphate dehydrogenase, NADP-dependent enzymes. The drug did not have an effect on succinate dehydrogenase, a flavoprotein. The Ki values with respect to substrate were 0.73, 0.3 and 3.5 microM for alpha-hydroxyacid, malate and glutamate dehydrogenases, respectively, and 1.1, 0.19 and 7.8 microM with respect to the coenzyme. Inhibition was noncompetitive with respect to substrate and uncompetitive in relation to the coenzyme.
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PMID:Inhibition by gossypol of oxidoreductases from Trypanosoma cruzi. 637 Feb 65

Histochemical analysis for NADP-dependent dehydrogenases, succinate dehydrogenase, NADH and NADPH- tetrazoleum reductases and esterase was conducted on primary cultures of adipose tissue stromal-vascular cells. Enzyme activities were restricted to clusters of lipid laden cells (adipocytes). The number of enzyme reactive adipocytes increased with length of culture. Coverslips were partially coated with collagen to allow comparisons of cell differentiation on coated (C-glass) and uncoated glass (U-glass) surface. There were no reactions for NADH- and NADPH- tetrazoleum reductases (TR) in cells on C-glass whereas adipocytes and stromal cells on U-glass were reactive. Glucose-6-phosphate (G6PDH) and 6-phosphogluconate (6PGDH) dehydrogenase activities were markedly demonstrated in both stromal cells and adipocytes on U-glass. Malate (MDH) and isocitrate (ICDH) dehydrogenase activities were higher in adipocytes than in stromal cells on the U-glass. Stromal cells on C-glass were either devoid of these enzymes (G6PDH, MDH, 6PGDH, ICDH) or activity was restricted to a small area of the cytoplasm. There were two levels of staining intensity in (MDH, ICDH, G6PDH, 6PGDH) adipocyte clusters on C-glass. Elimination of phenazine methosulphate from the NADP-dependent dehydrogenase medias and SDH media, caused a reduction in enzyme reactive adipocytes on the C-glass. This manipulation did not reduce the number of enzyme reactive cells on U-glass. Cells on C-glass and U-glass were distinctly different in esterase stained coverslips. These studies demonstrated enzyme histochemical reactions of adipocytes and stromal cells in primary culture that were dependent on the type of extracellular matrix. Furthermore, enzyme histochemistry was shown to be useful for delineating adipocytes from stromal cells in primary cultures.
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PMID:The histochemistry of developing adipocytes in primary stromal-vascular cultures of rat adipose tissue. 642 89

In porcine interareolar placental epithelia, the following enzymes were demonstrated by histochemical methods after 30, 58, 80, 100, and 110 d of pregnancy, respectively: beta-N-acetylhexosaminidase, beta-galactosidase, beta-glucuronidase, alpha-mannosidase, acid phosphatase, alkaline phosphatase, nonspecific esterases, cytochrome oxidase, 5-nucleotidase, leucine aminopeptidase, adenosine triphosphatase, diaphorases (NADH, NADPH), glucose-6-phosphate dehydrogenase, 6-phosphogluconate dehydrogenase, succinate dehydrogenase, isocitrate dehydrogenase (NAD, NADP), beta-hydroxybutyrate dehydrogenase, glycero-3-phosphate dehydrogenase, NAD-glycero-3-phosphate dehydrogenase, glutamate dehydrogenase (NAD, NADP), lactate dehydrogenase. The results show that most of the enzyme activities remained almost unchanged during the period of investigation. Only G-6-PDH and 6-PGDH activities increased within the uterine epithelium and nonspecific esterase activity within uterine as well as chorionic epithelia during the 2nd half of pregnancy. Within chorionic and uterine epithelia, hydrolases but not dehydrogenases demonstrated a higher activity at the bases of chorionic villi as compared to the apices and flanks of the latter. The action and influence of the demonstrated enzymes on metabolism, energy transfer, secretory, and resorptive activities of chorionic and uterine epithelia are discussed.
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PMID:[Enzyme histochemical studies of the swine placenta. Histoptics of enzymes in interareolar placental epithelia]. 643 35

The reductive carboxylation of 2-oxoglutarate was found to proceed in mitochondria of rat epididymal fat pads and rabbit perirenal adipose tissue at a rate similar to that in liver mitochondria. In rat fat pads the incorporation of 14C from [5-14C]2-oxoglutarate into fatty acids via the carboxylation was suppressed by butylmalonate by 30%. 2-Oxoglutarate and glutamate stimulated the incorporation into fatty acids of 14C from [2-14C]acetate in rat fat pads with the simultaneous reduction of tissue NADP. These effects persisted after inhibition of succinate dehydrogenase by malonate. It is concluded that in adipose tissue 2-oxoglutarate carboxylation proceeds in both the cytoplasm and mitochondria. Therefore, it can supply carbon atoms as well as NADPH for fatty acid synthesis.
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PMID:Intramitochondrial reductive carboxylation of 2-oxoglutarate in adipose tissue and its contribution to fatty acid synthesis. 653 9

Adipose tissue from fetuses decapitated at 45 d of gestation was removed and structurally and histochemically analyzed at 65, 85 and 110 d of gestation. Subcutaneous adipose tissue from decapitated and control fetuses at 65 d of gestation was histologically and histochemically similar. A reduced number of fat cell clusters in the outer layer of subcutaneous tissue and a poorly developed dermis was evident in decapitated fetuses at 85 d of gestation. Fat cell size was similar for control and decapitated fetuses at 65 d of gestation, whereas cells in 85 d-old decapitated fetuses were larger than cells in control fetuses. Adipocytes from control and 85 d-old decapitated fetuses were histochemically similar except for an elevated number of esterase positive cells in decapitated fetuses. At 110 d of gestation, adipocytes from decapitated fetuses had higher activities of the following enzymes than did control adipocytes: malate dehydrogenase (NADP dependent) glucose 6-phosphate dehydrogenase NADP dependent), isocitrate dehydrogenase (NADP dependent), alpha-glycerol phosphate dehydrogenase (NADP dependent), NADPH-tetrazoleum reductase and esterase. Levels of succinate dehydrogenase, glutamate dehydrogenase and NADH-tetrazoleum reductase were similar in cells from controls and decapitated fetuses. These data indicate that fetal decapitation probably exerts a positive influence on enzymes involved in lipid synthesis. However, fetal decapitation also exerts a negative influence on fat cell hyperplasia.
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PMID:Histochemical and cellular aspects of adipose tissue development in decapitated pig fetuses: an ontogeny study. 674 43


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