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)

Changes in carbohydrate metabolism were studied in midgut gland, muscle, and gill tissues of marine prawn Penaeus indicus exposed to a sublethal concentration (0.3 ppm) of phosphamidon. A significant decrease in glycogen and pyruvate and an increase in lactate content were observed in all phosphamidon-exposed prawn tissues after 96 hr. An increase in phosphorylase a and aldolase activity levels suggested the increased formation of triose sugars during phosphamidon toxicity. LDH activity was considerably decreased and an increment in lactate content was observed which indicates reduced mobilization of pyruvate into the citric acid cycle. Glucose-6-phosphate dehydrogenase activity was considerably increased, suggesting the enhanced oxidation of glucose in the hexose monophosphate shunt pathway. Krebs cycle enzymes such as NAD-isocitrate dehydrogenase, succinate dehydrogenase, and malate dehydrogenase were found to be decreased, suggesting the impairment in mitochondrial oxidative metabolism due to the acute toxic impact of phosphamidon. Cytochrome-c oxidase and Mg2+ ATPase activity levels were also decreased considerably, suggesting impaired energy synthesis and breakdown during phosphamidon toxicity, as a result of reduced oxidation of glucose aerobically. The increase in acid and alkaline phosphatase activities indicates the enhanced breakdown of phosphate to release energy in view of inhibiton or impairment in the ATPase system during phosphamidon-induced stress. These results suggest that phosphamidon has a profound effect on the oxidative metabolism of prawn which results in the triggering of compensatory metabolic pathways for survivability.
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PMID:Modulation of carbohydrate metabolism in the selected tissues of marine prawn, Penaeus indicus (H. Milne Edwards), under phosphamidon-induced stress. 337 38

A quantitative histochemical method (Trident) has been adapted to measure the activities of 4 enzymes, succinate dehydrogenase (SD), isocitrate dehydrogenase (ICD), glucose-6-phosphate dehydrogenase (G6PD) and 6-phosphogluconate dehydrogenase (6-PGD), within the liver acini of the rat during the postnatal developmental period. Quantitative changes of these enzymes in livers of rats of 25 g and 50 g body weight were studied, with particular emphasis on the activity-rest cycle. The results indicate a time-dependent heterogeneous distribution of enzymes along the acinar zones and the pattern of localization is age-dependent. When the mean enzyme activity from each group in relation to the time of the day are compared, a mirror image of each other could be seen. In general, a high enzyme activity has been observed during the resting phase in 25-g rats and low in 50-g rats. During the developmental period, the mean ICD activity is diminished, whereas G6PD and 6-PGD are augmented, and SD activity remains unchanged.
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PMID:Quantitative topochemistry of rat liver enzymes during postnatal development in relation to activity-rest cycle. 382 86

Polyacrylamide gel electrophoresis (PAGE) technique was standardised to demonstrate some key enzymes of glycolysis, hexose mono phosphate (HMP) pathway and tricarboxylic acid cycle in slow growing mycobacteria (M. avium. M. gastri) as well as in fast growing mycobacteria (M. vaccae, M. phlei). The enzymes studied were lactate dehydrogenase (LDH) glucose-6-phosphate dehydrogenase (G6PD), aconitase, isocitrate dehydrogenase (ICD), succinic dehydrogenase (SDH), fumerase and malate dehydrogenase (MDH). All the three pathways were found to be operative in slow as well as fast growing mycobacteria. Using this technique M. leprae specific MDH activity was demonstrated in the cell free extract of M. leprae. It's (MDH) electrophoretic mobility on gels lies in the range shown by other mycobacterial species studied and was distinct from that of host MDH. It appears that PAGE offers a useful tool for metabolic characterization of M. leprae using infected tissues.
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PMID:Metabolic studies on mycobacteria-I. Demonstration of key enzymes of glycolysis and tricarboxylic acid cycle on polyacrylamide gels. 383 Oct 90

In porcine areolar placental epithelia, the following enzymes were demonstrated by histochemical methods after 30, 58, 80, 100, and 110 d of pregnancy, respectively: beta-N-acetyl-hexosaminidase, 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 the enzyme activities remained almost unchanged during the period of investigation. Of the dehydrogenases, the diaphorases as well as succinate and lactate dehydrogenase demonstrated generally an intensive activity within the epithelia. The activity of the other dehydrogenases was only low. The activity of unspecific esterase was very intensive within the uterine epithelia but remarkably low within chorionic epithelia. Contrarily, the reaction of adenosine triphosphatase was more intensive within chorionic than uterine epithelia. All investigated glucosidases reacted distinctly positive within chorionic epithelia, but only beta-N-acetyl-hexosaminidase and beta-galactosidase in uterine epithelia. The high activity of acid phosphatase, especially within the chorionic epithelium, seems to be connected with uteroferrin, an iron-binding protein. The histochemical results are discussed in context with the function of the areolae in histiotrophic nutrition and iron transport.
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PMID:[Enzyme-histochemical studies of the pig placenta. II. Histotopics of enzymes in the areolar placenta epithelium]. 392 41

Histochemical investigation of altered dehydrogenase enzyme activity in putative pre-neoplastic lesions induced by N-ethyl-N-hydroxyethylnitrosamine in the rat liver revealed a clear increase in NADPH-generating potential, most markedly within nodules. Glucose-6-phosphate dehydrogenase, malic enzyme and isocitrate dehydrogenase all showed elevated activity while the activities of succinate dehydrogenase and beta-hydroxybutyrate dehydrogenase were reduced. Alteration in enzyme activity suggested an adaptive shift in metabolism, the increase in levels of enzymes responsible for generation of reduced NADP possibly conferring enhanced drug detoxifying or cholesterogenic potential.
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PMID:Dehydrogenase histochemistry of N-ethyl-N-hydroxyethylnitrosamine-induced focal liver lesions in the rat--increase in NADPH-generating capacity. 394 19

Fetuses were decapitated in one uterine horn in each of 14 sows at 45 d of gestation. Control (C) and decapitated (D) fetuses were removed by Caesarean section from three sows at 65 d of gestation (total of 10 D and 10 C fetuses), two sows at 85 d (six D and six C fetuses) and nine sows at 110 d (nine C and nine D fetuses) of gestation (Exp. 1). In Exp. 2, four to six fetuses were removed from each of two Ossabaw (O) gilts and three crossbred (C, Landrace X Yorkshire) gilts at 70 d of gestation, from three C and O gilts at 90 d of gestation and from three C and two O gilts at 110 d of gestation. In Exp. 1, one semitendinosis muscle was removed for histochemistry, whereas the contralateral muscle was removed and weighed. A medial portion of biceps femoris muscle was removed and used for histochemistry in Exp. 2. In both experiments, transverse sections (cryostat) of muscle were stained for lipid, glycogen (PAS) and the following enzymes: acid ATPase, NADH-TR, NADPH-TR, malate dehydrogenase (NAD- and NADP-dependent reactions; MDH), succinate dehydrogenase (SDH), alpha-glycerol phosphate dehydrogenase (with and without NAD; alpha-GPDH), isocitrate dehydrogenase (NAD dependent; ICDH), esterase, lipoprotein lipase and lipase. In Exp. 1, body and muscle weights of the two groups were not significantly different (P greater than .05) at 65 d of gestation, whereas D fetuses were smaller and had lighter weight muscles (P less than .05) at 85 d of gestation.(ABSTRACT TRUNCATED AT 250 WORDS)
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PMID:Enzyme histochemical studies in an ontogeny study of muscle development in Ossabaw and decapitated fetuses: cellular reactions. 401 46

The intracellular distribution of enzymes of the TCA cycle was investigated in liver of rainbow trout. All enzymes of the cycle apart from succinyl thiokinase were detected. Citrate synthase, alpha-ketoglutarate dehydrogenase and succinate dehydrogenase were wholly mitochondrial. Fumarase, malate dehydrogenase, aconitase and NADP-isocitrate dehydrogenase were detected in both cytosol and mitochondria.
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PMID:Intracellular distribution of tricarboxylic acid cycle enzymes in liver of rainbow trout Salmo gairdneri. 405 77

1. Increased specific activities of cytochrome c oxidase, catalase, succinate dehydrogenase, succinate-cytochrome c oxidoreductase, NADH-cytochrome c oxidoreductase and malate dehydrogenase were observed during glucose de-repression of Schizosaccharomyces pombe. 2. The cell-cycle of this organism was analysed by three different methods: (a) harvesting of cells at intervals from a synchronous culture, (b) separation of cells by rate-zonal centrifugation into different size classes and (c) separation of cells by isopycnic-zonal centrifugation into different density classes. 3. Measurement of enzyme activities during the cell-cycle showed that all the enzymes assayed [cytochrome c oxidase, catalase, acid p-nitrophenylphosphatase, NADH-dehydrogenase, NADH-cytochrome c oxidoreductase, NADPH-cytochrome c oxidoreductase, succinate dehydrogenase, malate dehydrogenase, isocitrate dehydrogenase (NADP) and fumarate hydratase] show periodic expression as ;peaks'. 4. Cytochrome c oxidase shows a single maximum at 0.67 of a cycle, whereas succinate dehydrogenase exhibits two maxima separated by 0.5 of a cell-cycle. 5. All other enzymes assayed showed two distinct maxima per cell-cycle; for catalase, malate dehydrogenase and NADPH-cytochrome c oxidoreductase there is the possibility of multiple fluctuations. 6. The single maximum of cytochrome c oxidase appears at a similar time in the cycle to one maximum of each of the other enzymes studied, except for NADH dehydrogenase. 7. These results are discussed with reference to previous observations on the expression of enzyme activities during the cell-cycle of yeasts.
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PMID:Oscillations of enzyme activities during the cell-cycle of a glucose-repressed fission-yeast Schizosaccharomyces pombe 972h-. 414 72

1. Changes in the amounts and distribution of protein and respiratory enzymes have been estimated during the life cycle of the fly Lucilia cuprina. 2. The fully fed larva contains about 7mg. of protein, the pupa and newly emerged fly about 4mg., and the mature adult about 3mg. 3. There are two periods of incorporation of protein into particles at the expense of the soluble protein; the first, immediately after pupation, may store protein (0.5mg./insect) for use in adult development; the second, over the period of emergence, was due mainly to the development of the thoracic mitochondria of the adult (0.7mg./insect). 4. In the thorax, cytochrome c oxidase and the dehydrogenases for glycerophosphate, isocitrate (NAD-dependent), succinate and malate appeared initially in small particles (less than 1mu in diameter). 5. In adult development these enzymes were redistributed so that in the mature fly most of the activity was present in larger particles (1-10mu in diameter). 6. During this redistribution the specific activity (mul. of oxygen/hr./mg. of protein) of glycerophosphate dehydrogenase in the small particles was 690 at 1(1/2) days before emergence, 955 at emergence and 980 at 7 days after emergence; the corresponding values for the large particles were 164, 760 and 1220. 7. In the mature fly the highest specific activities (mul. of oxygen/hr./mg. of protein) estimated were: glycerophosphate dehydrogenase 1380, isocitrate dehydrogenase (NAD-dependent and requiring ADP and Mg(2+)) 408, succinate dehydrogenase 122, malate dehydrogenase 190, and cytochrome c oxidase 1360. 8. The results are considered in relation to the development of the flight-muscle sarcosomes.
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PMID:Aspects of the development of flight-muscle sarcosomes in the sheep blowfly, Lucilia cuprina, in relation to changes in the distribution of protein and some respiratory enzymes during metamorphosis. 429 61

Crude extracts of both vegetative cells and glycerol-induced microcysts of Myxococcus xanthus contained the following enzyme activities: phosphofructokinase, phosphoglucoisomerase, fructose-1,6-diphosphatase, fructosediphosphate aldolase, glyceraldehyde-3-phosphate dehydrogenase, phosphopyruvate carboxylase, citrate synthase, isocitrate dehydrogenase, alpha-ketoglutarate dehydrogenase, succinate dehydrogenase, malate dehydrogenase, glucose-6-phosphate dehydrogenase, 6-phosphogluconate dehydrogenase, phosphoglucomutase, and uridine diphosphate glucose pyrophosphorylase. With the exception of isocitrate dehydrogenase, which was present at a fivefold higher concentration in microcysts, all activities in extracts from both types of cells were essentially equal. Hexokinase and pyruvate kinase could not be detected in extracts from either type of cell. Microcysts metabolized acetate at a lower rate than did vegetative cells. Most of this decrease was reflected in a substantial decrease in ability of microcysts to oxidize acetate to CO(2). In addition, microcysts and vegetative cells showed a different distribution of (14)C-label from incorporated acetate.
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PMID:Comparative intermediary metabolism of vegetative cells and microcysts of Myxococcus xanthus. 430 96


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