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)

Dose-dependent increases in alkaline phosphatase and acid phosphatase activities, decreases in myeloperoxidase activity of neutrophils and depression of lymphocyte glycerophosphate dehydrogenase and succinate dehydrogenase activities were discovered in rat nephropathy induced by mercuric chloride at doses of 0.1-1.0 mg/kg. These changes manifest the intensity of the oxidation-reduction process, the reduction of Kreb's cycle and alpha-glycerophosphatic shunt, the damage by peroxidation and the increase in catabolic processes. The morphometric data of nephron structure reflected the functional cell stress and they were compared with leucocyte enzyme status changes.
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PMID:Some aspects of testing drugs for nephrotoxicity in rats. 677 35

Data are presented from cytochemical study of the neutrophil myeloperoxidase oxygen dependent enzymes and lymphocyte succinate dehydrogenase in the peripheral blood of 2169 persons subjected to follow-ups of many kinds, at year 7 and 8 after the Chernobyl accident. By comparison with early time periods, the process of normalization of the measured values has been found to be the case, with SDG returning to normal earlier than MPO. There was an increase in the number of individuals with reduced MPO activity and stable percentage of those demonstrating increased SDG activity (30-42% versus 12%). Significance of the adaptation process in the time course of changes of the values measured is discussed along with role of hypoxic factor in adaptation to the ionizing irradiation exposure after the Chernobyl accident.
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PMID:[The significance of the hypoxic factor in adaptation to the action of ionizing radiation as a result of the accident at the Chernobyl Atomic Electric Power Station]. 760 84

Succinate oxidation in scutella of germinating seeds of wheat and maize was investigated. Besides oxidation via succinate dehydrogenase (SDH; EC 1.3.99.1), an alternative path of succinate oxidation insensitive to SDH inhibitors--malonate and thenoyltrifluoroacetone (TTFA)--was revealed. Using isopicnic sucrose gradient it was shown that this path is localized in glyoxysomal membranes. Glyoxysomal succinate oxidase (GSO) converts succinate directly into malate with the production of hydrogen peroxide identified using auxiliary enzymes malate dehydrogenase and peroxidase. GSO is most active during the intensive operation of the glyoxylate cycle (3-5 days of germination). Quinacrine, the inhibitor of flavine-containing oxidases, strongly suppressed the activity of GSO. Km for succinate is 18 mM for GSO from maize scutellum. It is concluded that in scutella of cereal seeds the glyoxysomal succinate oxidation non-linked with ATP synthesis operates.
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PMID:Alternative system of succinate oxidation in glyoxysomes of higher plants. 760 25

Site-directed mutagenesis has been used to introduce cysteine residues into yeast cytochrome c peroxidase and yeast cytochrome c for the purpose of forming site-specific cross-linked intermolecular complexes. This enables the formation of well-defined homogeneous covalently linked complexes for the purpose of relating structure to intramolecular electron transfer. Two complexes have been prepared and analyzed. Complex I has an engineered cysteine at position 290 near the C-terminus of the peroxidase linked to the naturally occurring Cys102 near the C-terminus of yeast cytochrome c. This complex exhibits undetectable rates of intramolecular electron transfer. Complex II has Cys290 of the peroxidase linked to the engineered Cys73 of cyt c. This complex was designed to mimic the crystal structure of the peroxidase-cytochrome c noncovalent complex [Pelletier & Kraut (1992) Science 258, 1748-1755]. Stopped-flow studies show that complex II carries out intramolecular electron transfer from ferrocytochrome c to peroxidase compound I at a rate of approximately 500-800 s-1. This indicates that the binding orientation observed in the crystal structure is competent in rapid intramolecular electron transfer.
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PMID:Site-specific cross-linking as a method for studying intramolecular electron transfer. 775 88

Submandibular glands obtained post-mortem from mature ferrets of both sexes were examined with the use of light microscopical histochemical methods for proteins, mucosubstances and enzymes associated with cell functions or organelles. Demilunar cells showed carboxylated mucosubstances that were mainly non-sulphated, and diffuse activity for peroxidase, E600-sensitive esterase and acid phosphatase. Thiol groups were also detected in these cells. Central acinar cells showed sulphated mucosubstances, disulphides and reticular staining for thiamine pyrophosphatase. Intercalary ducts showed diffuse activity for NADH and NAD(P)H dehydrogenases. Striated ducts contained protein, tryptophan, disulphides, neutral mucosubstances and E600-sensitive esterase periluminally. Basally, the striated ductal cells showed variable activity for peroxidase, cytochrome oxidase, succinate dehydrogenase and acid phosphatase. Basolateral plasma membranes of these cells exhibited ouabain-sensitive Na,K-ATPase activity. The collecting ducts were characterized by variable periluminal staining for acid phosphatase, beta-glucuronidase, acid beta-galactosidase and E600-resistant esterase. The results suggest that the histological appearances of the acini of the submandibular gland of the ferret are dependent on the synthesis of secretory acid glycoproteins, that the striated ducts are involved with the secretion of tryptophan-rich product comprising neutral glycoproteins and showing esterase activity and with marked transport of ions and that the collecting ducts are involved with absorption.
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PMID:Morphological phenotypes and functional capabilities of submandibular parenchymal cells of the ferret investigated by protein, mucosubstance and enzyme histochemistry. 1066 22

We studied the activity of NADP-dependent isocitrate dehydrogenase, malate dehydrogenase, succinate dehydrogenase, catalase, and peroxidase as well as the rate of 14CO2 release after introduction of labeled substrates for glycolysis and citrate acid cycle within 24 h after salt stress (1% NaCl) in 10-14 days old germinants of wheat (Triticum aestivum L.) and maize (Zea mays L.) as well as thallus of small duckweed (Wolffia arrhiza (L.) Hork ex Wimmer). Oscillations in the enzymes activity with 4-6 h period have been revealed under stress conditions. Activity of glycolysis decreased in wheat and maize and increased in duckweed under the influence of stress stimulus. Six hours after NaCl action decarboxylation of exogenous citrate and succinate was enhanced in all three plants while the rate of exogenous malate decarboxylation was decreased. We conclude that adaptation of higher plans to salinization is accompanied by rearrangements in oxidative metabolism reflected by oscillations in activity of the enzymes involved in oxidative metabolism.
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PMID:[Effect of salt stress on respiration metabolism in higher plants]. 1086 56

Von Ebner's gland of ferret was examined by means of light microscopy, protein, mucosubstance and enzyme histochemistry, and neurohistology. Acinar cells were replete with granules containing neutral mucosubstances and disulphides, and showed strong diffuse acid phosphatase activity and weak granular staining for peroxidase. Staining for cytochrome oxidase, succinate dehydrogenase, and NADH and NAD(P)H dehydrogenases was also seen. Basolateral plasmalemma of acinar cells showed weak, ouabain-sensitive Na+,K+-ATPase activity. Ductal cells were of a simple appearance, contained thiols and showed variable staining for acid phosphatase, dehydrogenases and cytochrome oxidase. Variable amounts of beta-glucuronidase reaction product were localized in the glandular parenchyma, being marked in atrophic areas. Prominent stellate myoepithelial cells embracing acini and also basal ductal cells were demonstrated by alkaline phosphatase. Thiamine pyrophosphatase reaction product was concentrated in blood vessels around parenchyma, with little Golgi-like staining in acinar cells. Acetylcholinesterase activity was associated with an extensive network of nerve fibres embracing parenchyma, whereas catecholamine fluorescence was not seen. The results suggest that the acini of von Ebner's gland of ferret synthesise neutral secretory glycoproteins and peroxidase. Water mobilization is inconspicuous. Lysosomal activities feature in the parenchyma, possibly a consequence of processing secretory products in acini, absorption in ducts and/or adaptation atrophy. The gland receives a rich cholinergic-type innervation, and has extensive myoepithelial and microvascular networks.
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PMID:Histochemical phenotypes of von Ebner's gland of ferret and their functional implications. 1150 41

Mitochondria are widely believed to be the source of reactive oxygen species (ROS) in a number of neurodegenerative disease states. However, conditions associated with neuronal injury are accompanied by other alterations in mitochondrial physiology, including profound changes in the mitochondrial membrane potential DeltaPsi(m). In this study we have investigated the effects of DeltaPsi(m) on ROS production by rat brain mitochondria using the fluorescent peroxidase substrates scopoletin and Amplex red. The highest rates of mitochondrial ROS generation were observed while mitochondria were respiring on the complex II substrate succinate. Under this condition, the majority of the ROS signal was derived from reverse electron transport to complex I, because it was inhibited by rotenone. This mode of ROS generation is very sensitive to depolarization of DeltaPsi(m), and even the depolarization associated with ATP generation was sufficient to inhibit ROS production. Mitochondria respiring on the complex I substrates, glutamate and malate, produce very little ROS until complex I is inhibited with rotenone, which is also consistent with complex I being the major site of ROS generation. This mode of oxidant production is insensitive to changes in DeltaPsi(m). With both substrates, ubiquinone-derived ROS can be detected, but they represent a more minor component of the overall oxidant signal. These studies demonstrate that rat brain mitochondria can be effective producers of ROS. However, the optimal conditions for ROS generation require either a hyperpolarized membrane potential or a substantial level of complex I inhibition.
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PMID:DeltaPsi(m)-Dependent and -independent production of reactive oxygen species by rat brain mitochondria. 1167 54

A study of the action of different physical factors on micro-organisms is necessary for a further development of exobiology. The action of temperature on crystalline preparations of catalase and peroxidase was studied by means of oscillographic polarography. A determination of the height of polarographic waves at the decrease of temperature from 20 degrees C to 0 degrees C has shown that structural elements of the peroxidase molecule connected with the enzymatic activity are more stable with the decrease of temperature cf. catalase. A relative resistance of the dehydrogenase activity in Az. vinelandii cells to high vacuum was found. Incubation of azotobacter cells under vacuum of 10(-9) mm Hg during 72 hr did not decrease the activity of alcohol and succinic dehydrogenase. Bac. cereus spores can be preserved from bactericidal UV action by thin films of chrome. The thickness of chrome film being 200-670 angstroms, spores are killed by a dose of 7.8 x 10(7) erg/cm2 at 253.7 microns wave length. Spores covered by chrome film thicker than 800 angstroms remain alive after this treatment. Investigations carried out with an 'Artificial Mars' camera led to the following results. The growth of Bac. megaterium on liquid growth media in this camera ceases as a result of UV rays killing all cells after 3 weeks. Untreated bacteria grow in the camera for a long time. Spore-forming bacteria isolated from the sand of the Kara-Kum Desert grow in ground limonite (with the addition of 2% garden soil) having maximum hygroscopic humidity (3.8%). Freezing and thawing (from -60 degrees C to +25 degrees C) corresponding to day temperature deviations on Mars, low pressure (P=10 mm Hg) and the composition of the atmosphere (CO2-50%, N2-40%, Ar-10%) do not influence the growth of xerophylic bacteria under study. Humidity is the main factor limiting the growth of micro-organisms under 'Artificial Mars' conditions. According to the further development of the microbiological meteorite analysis methods, samples of rocks and stone meteorites were sterilized, incubated in the desert or on a snow surface in the Arctic and after different times (from 100 days to 7 months), investigated. In all cases, microbes were found only on the sample surfaces, whereas 1 cm from the surface and in the central parts micro-organism were completely absent. Hence, microbiological analysis of central parts of meteorites fallen in the Arctic or during dry periods of the year in the desert can give reliable results.
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PMID:Exobiology and the effect of physical factors on micro-organisms. 1197 48

Although human cancers are widely treated with anthracycline drugs, these drugs have limited use because they are cardiotoxic. To clarify the cardiotoxic action of the anthracycline drug adriamycin (ADM), the inhibitory effect on succinate dehydrogenase (SDH) by ADM and other anthracyclines was examined by using pig heart submitochondrial particles. ADM rapidly inactivated mitochondrial SDH during its interaction with horseradish peroxidase (HRP) in the presence of H(2)O(2) (HRP-H(2)O(2)). Butylated hydroxytoluene, iron-chelators, superoxide dismutase, mannitol and dimethylsulfoxide did not block the inactivation of SDH, indicating that lipid-derived radicals, iron-oxygen complexes, superoxide and hydroxyl radicals do not participate in SDH inactivation. Reduced glutathione was extremely efficient in blocking the enzyme inactivation, suggesting that the SH group in enzyme is very sensible to ADM activated by HRP-H(2)O(2). Under anaerobic conditions, ADM with HRP-H(2)O(2) caused inactivation of SDH, indicating that oxidized ADM directly attack the enzyme, which loses its activity. Other mitochondrial enzymes, including NADH dehydrogenase, NADH oxidase and cytochrome c oxidase, were little sensitive to ADM with HRP-H(2)O(2). SDH was also sensitive to other anthracycline drugs except for aclarubicin. Mitochondrial creatine kinase (CK), which is attached to the outer face of the inner membrane of muscle mitochondria, was more sensitive to anthracyclines than SDH. SDH and CK were inactivated with loss of red color of anthracycline, indicating that oxidative activation of the B ring of anthracycline has a crucial role in inactivation of enzymes. Presumably, oxidative semiquinone or quinone produced from anthracyclines participates in the enzyme inactivation.
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PMID:Inactivation of mitochondrial succinate dehydrogenase by adriamycin activated by horseradish peroxidase and hydrogen peroxide. 1260 55


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