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)

A method is described for the preparation of spheroplasts in high yield from Schizosaccharomyces pombe, by treating cells grown in the presence of glucose and deoxyglucose with snail digestive enzymes. Gentle disruption of such spheroplasts yielded homogenates, from which marker enzymes for nuclei (NAD pyrophosphorylase) and mitochondria (cytochrome c oxidase activity and spectroscopically-detectable cytochromes a + a3) could be quantitatively sedimented by low-speed centrifugation. In contrast to previous findings with Saccharomyces carlsbergensis, cytochrome c oxidase and another mitochondrial enzyme, succinate dehydrogenase, were completely sedimentable by zonal centrifugation in sucrose gradients in the presence of either 2 mM-MgCl2 or 0-4 mM-EDTA. Mitochondria were apparently smaller and of lower buoyant density in gradients containing EDTA. The bulk of the total units of malate dehydrogenase and NADH; cytochrome c oxidoreductase sedimented with mitochondria, whereas NADPH: cytochrome c oxidoreductase was located in fractions containing no mitochondria. The distributions of mitochondrial enzymes were heterogeneous in populations of mitochondria separated on the basis of size or density. The possible origins of mitochondrial heterogeneity in extracts of S. pombe are discussed with special reference to changes in the enzyme activities of cells during the cell cycle.
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PMID:Fractionation by differential and zonal centrifugation of spheroplasts prepared from a glucose-repressed fission yeast Schizosaccharomyces pombe 972h-. 18 Feb 35

Activities of succinate dehydrogenase, succinate- and NAD-H-cytochrome c--reductases, and cytochrome c--oxidase was compared in 1 g tissue homogenate and homogenate fractions made from 1 g brain tissue using various solutions. Fractionation resulted in the increased activities of NADH- and succinate cytochrome reductases, and in the loss of succinate dehydrogenase activity, cytochrome oxidase was less influenced. These phenomena are regarded as signs of the interrelation between mitochondria and other constituents of brain cell within homogenates. Maximal quantity of mitochondria isolated from homogenates is no more than 20% of all the mitochondrial homogenates (according enzyme data). The electronogram of the brain mitochondrial preparation isolated in the Krebs--Ringer solution without glucose pointed out to a high homogeneity of mitochondria in the residue.
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PMID:[Enzyme, electron microscopic and polarographic characteristics of isolated rat brain mitochondria. III. Quantitative assessment of their distribution in fractions of the homogenate]. 18 80

Acute renal failure was induced in male rats by the subcutaneous injectioon of 4 mg HgC12 per kg body weight. Enzyme activities of the proximal tubule were studied histochemically at six time intervals from 15 min to 24 h. The enzyme studied were alkaline phosphatase, 5'-nucleotidase, acid phosphatase, alpha-glycerophosphate dehydrogenase (NAD-independent), malic dehydrogenase, succinic dehydrogenase, latic dehydrogenase, glucose-6-phosphate dehydrogenase and glucose-6-phosphatase. Decreases in activity were observed for alkaline phosphatase and 5'-nucleotidase after 15 min. Acid phosphatase was decreased after 30 min. These three enzymes returned to control levels after 3 h, but malic dehydrogenase and alpha-glycerophosphate dehydrogenase were decreased at this time interval. Succinic dehydrogenase was first decreased after 6 h. The earliest morphological changes detectable by light microscopy were observed in pars recta tubules in the medullary rays after 6 h, a time when all enzymes studied showed widespread decreased activity throughout the proximal tubule. After 24 h, the pars convoluta appeared morphologically normal but the pars recta was necrotic and exhibited calcification, whereas enzyme activity was decreased (absent in some cases) in both pars convoluta and pars recta. These results support the hypothesis that Hg++, when given in a sublethal dose, is associated with early histochemical changes in the brush border of the proximal tubule, which may be related to early changes in sodium reabsorption and to the subsequent development of acute renal failure. The observation that changes in plasma membrane-associated enzymes occur early and prior to alterations in enzymes of mitochondria and the endoplasmic reticulum suggests that Hg++ interacts initially with the plasma membrane.
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PMID:Studies on the pathophysiology of acute renal failure. II. A histochemical study of the proximal tubule of the rat following administration of mercuric chloride. 18 27

Histochemical methods were used for the demonstration of activity of the following intracellular oxidative enzymes, unstudied hitherto, in the epithelial cells of the endostyle of the river lampre (Lampertr aluviatilis L.) ammocoetes: reduced NAD dehydrogenase (NADD), lactate dehydrogenase (LD), cytochrome oxidase (CO), succinate dehydrogenase (SD), alpha-glycerophosphate dehydrogenase (alphaGPD) and glucose-6-phosphate dehydrogenase (G6PD). The activities of NADD and LD in the iodophil and throidogenic cells of type 3, then of subtype 2c and partly types 4 and 5 of the endostylar epithelium and the hypobranchial duct-lining epithelium were particularly ithe larva proves the possibility of their participation in the formation of the thyroid gland in the period of metamorphosis. In type 1 cells of the ammocoetes, despite their fairly strong enzymatic reactivity, the oxidative activity does not change significantly during the ontogenetic stages examined. The data obtained make it possible to modify the present views on the genesis of the thyroid gland of the adult lamprey, namely, they indicate the participation of the type 6 cells of the hypobranchial duct-lining epithelium in the process of thyroidogenesis.
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PMID:The ammocoetes endostyle: its oxidative enzymes as an evidence of its homology with the thyroid of higher chordates. 19 46

Histochemical methods were used to investigate the activities of some intracellular enzymes in the oral mucosa of the rabbits which had been kept in selected work-stands of a coking-plant for 3 months. The findings were compared with the results for the enzymatic activity of the oral mucosa of control rabbits. The epithelium of the oral mucosa of the experimental rabbits was found to be proliferated acanthotically; moreover, there occurred some other morphological changes of the mucosa which often resembled precancerous states of leukoplakia type. In comparison with the control group, the activities of the studied enzymes, i.e. reduced NAD dehydrogenase (NADD), glucose-6-phosphate dehydrogenase (G6PD), lactate dehydrogenase (LDS), succinate dehydrogenase (SD), cytochrome oxidase (CO), and phosphorylase a+b in the epithelium and the connective-tissue cells of the studied mucosa of the experimental animals were as a rule markedly lowered, this decline being especially pronounced for the three last-mentioned enzymes. It was only the proliferating stratum basale of the experimental rabbit epithelium that frequently exhibited enhanced activities of NADD and LDS. Besides, the activities of NADD, G6PD and LDS were of a markedly diverse intensity in the cells of the chaotically proliferating stratum spinosum of the experimental rabbit mucosa. The results point to the noxious modifying effect of chemical and physical agents of the investigated environment on the oral mucosa of the animals studied.
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PMID:The effect of environmental factors of the coking plant on the enzymatic activity of rabbit oral mucosa. 19 66

The distribution and activities of several oxidative enzymes in various regions of the sebaceous glands of the domestic cat have been studied. The results obtained emphasize the outstanding importance of NADP-linked dehydrogenases for lipogenesis during sebum production. In particular, the reactions for glucose-6-phosphate dehydrogenase were very strong. Among the NAD-linked dehydrogenases investigated, lactate dehydrogenase showed strong activity in the peripheral cells of the sebaceous gland. The reactions for cytochrome oxidase and succinate dehydrogenase were weaker.
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PMID:Oxidative enzymes in the sebaceous glands of the domestic cat. 19 9

In 175 dogs myocardial infarction was produced by high ligation of descending branch of left coronary artery. At various intervals after the intervention (1, 3, 5, 10, 30, 180 days), the activities and levels of NAD, NADH, FAD, riboflavin, cytochrome C, myoglobin, some NAD-dependent Krebs cycle enzymes, and mitochondrial succinate dehydrogenase and cytochrome oxidase were determined in the infarcted zone. It was found that in the infarcted zone there occurred substantial disturbances of various links constituting the tissue oxidative chain, in the stages of substrate dehydrogenation, electron transport to oxygen molecule, and myocardial oxygen uptake. The greatest disturbances took place in the systems of NAD and NAD-dependent enzymes, whereas the succinate oxidation system sustained substantially lesser damage. The decrease inlevels of flavonoids, which was likewise observed, participated also in the mechanism inhibiting succinate dehydrogenase. The cytochrome system activity was limited by the level of cytochrome C, whose deep decrease persisted considerably long in the infarcted zone. A certain role in disturbances of oxidative processes may have been played by the decreased concentration of myoglobin, an important myocardial reservoir of oxygen.
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PMID:Some myocardial factors of biological oxidation in experimental myocardial infarction. 19 79

Characterization of the energy metabolism pattern of the specialized heart muscle of bovine heart was studied in comparison with that of the ordinary heart muscle. Mitochondrial oxygen consumption of the specialized heart muscle was significantly lower than that of the ordinary heart muscle with succinate as the substrate. On the other hand, there was no significant difference in oxygen consumption between both heart muscles with glutamate + malate as the substrates. The activity levels of succinate dehydrogenase and lactate dehydrogenase were much lower than those of the ordinary heart muscle. The isozyme pattern of LDH of the specialized heart muscle consisted of one major component of LDH-1 (H4) and that of the ordinary heart muscle consisted of two major components of LDH-1 (H4) and LDH-2 (H3M). The ratio of NADH to NAD of the specialized heart muscle was remarkably lower than that of the ordinary heart muscle. These results indicate that the specialized heart muscle depends not only upon anaerobic metabolism but also upon aerobic metabolism for its energy supply.
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PMID:Characteristics of energy metabolism in specialized muscle of bovine heart. 20 90

1. The properties of membrane vesicles from the extreme thermophile Bacillus caldolyticus were investigated. 2. Vesicles prepared by exposure of spheroplasts to ultrasound contained cytochromes a, b and c, and at 50 degrees C they rapidly oxidized NADH and ascorbate in the presence of tetramethyl-p-phenylenediamine. Succinate and l-malate were oxidized more slowly, and dl-lactate, l-alanine and glycerol 1-phosphate were not oxidized. 3. In the absence of proton-conducting uncouplers the oxidation of NADH was accompanied by a net translocation of H(+) into the vesicles. Hydrolysis of ATP by a dicyclohexylcarbodi-imide-sensitive adenosine triphosphatase was accompanied by a similarly directed net translocation of H(+). 4. Uncouplers (carbonyl cyanide p-trifluoromethoxyphenylhydrazone or valinomycin plus NH(4) (+)) prevented net H(+) translocation but stimulated ATP hydrolysis, NADH oxidation and ascorbate oxidation. The last result suggested an energy-conserving site in the respiratory chain between cytochrome c and oxygen. 5. Under anaerobic conditions the reduction of cytochrome b by ascorbate (with tetramethyl-p-phenylenediamine) was stimulated by ATP hydrolysis, indicating an energy-conserving site between cytochrome b and cytochrome c. However, no reduction of NAD(+) supported by oxidation of succinate, malate or ascorbate occurred, neither did it with these substrates in the presence of ATP under anaerobic conditions, suggesting that there was no energy-conserving site between NADH and cytochrome b. 6. Succinate oxidation, in contrast with that of NADH and ascorbate, was strongly inhibited by uncouplers and stimulated by ATP hydrolysis. These effects were not observed when phenazine methosulphate, which transfers electrons from succinate dehydrogenase directly to oxygen, was present. It was concluded that in these vesicles the oxidation of succinate was energy-dependent and that the reoxidation of reduced succinate dehydrogenase was dependent on the outward movement of H(+) by the protonmotive force. 7. In support of the foregoing conclusion it was shown that the reduction of fumarate by NADH was an energy-conserving process. 8. If the activities of vesicles accurately represent those of the intact organism it appears that in B. caldolyticus the reduction of fumarate to succinate at the expense of reducing equivalents from NADH is energetically favoured over succinate oxidation even under aerobic conditions. This may be related to the need for an ample supply of succinate for haem synthesis in order to provide cytochromes for the organism.
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PMID:The oxidative activities of membrane vesicles from Bacillus caldolyticus. Energy-dependence of succinate oxidation. 20 11

Experiments were conducted on rabbits. A study was made of the activity of the redox enzymes--glucose-6-phosphate dehydrogenase (G-6-PDH), lactate dehydrogenase (LDH), succinate dehydrogenase (SDH), malate dehydrogenase (MDH), NAD-and NADP-diaphorases, cytochromeoxidase (CCO), alpha-glycerophosphate dehydrogenase (alpha-GPDH) in the supraoptic and paraventricular nuclei of the hypothalamus and the posterior lobe of the hypophysis under conditions of stimulation and removal of the superior cervical sympathetic ganglia. There was revealed a correlation between the activity of the tissue respiration enzymes (SDH, MDH, NAD- and NADP-diaphorase, CCO) and the functional condition of the hypothalamo-neurohypophysial neurosecretory system. However, the enzymes of the pentose-phosphate (G-6-PDH) and glycerophosphate shunt (alpha-GPDH) and also of the anaerobic way of oxidation (LDH) reacted nonspecifically on the induced effects.
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PMID:[Effect of removal and stimulation of the superior cervical sympathetic ganglia on the activity of oxidation-reduction enzymes in the neurosecretory cells of the anterior hypothalamus in rabbits]. 20 40


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