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)

The effects of zinc on the enzymes of femoral tissue were investigated in weanling rats that had been given zinc sulfate (1.0 mg Zn2+/100 g body wt) p.o. for 3 days. Administration of zinc caused a marked elevation of alkaline phosphatase and acid phosphatase activities, whereas it did not cause significant changes in succinate dehydrogenase, 5'-nucleotidase, ATPase, pyrophosphatase and beta-N-acetylglucosaminidase activities. The effect of zinc was greater on alkaline phosphatase of the femoral diaphysis. Zinc content of the femoral diaphysis was raised significantly by administration of zinc. The addition of zinc in concentrations of 10(-2)-10(2) microM did not produce a significant increase in alkaline phosphatase activity in the femoral diaphysis, indicating that zinc could not activate the enzyme. Administration of cycloheximide or actinomycin D completely inhibited the increase in alkaline phosphatase activity produced by administration of zinc. DNA content of the femoral diaphysis, but not epiphysis, was increased markedly by administration of zinc. The increases in both alkaline phosphatase activity and DNA content of the femoral diaphysis were not caused by administration of copper, manganese, cobalt, nickel and chromium(III). The present investigation suggests that zinc may induce the increase in alkaline phosphatase related to DNA synthesis and, as a result, stimulate bone growth.
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PMID:Action of zinc on bone metabolism in rats. Increases in alkaline phosphatase activity and DNA content. 395 86

The possible role of succinic dehydrogenase (SD) in producing physical dependence to morphine by affecting tissue respiration was investigated in Swiss albino mice during the development of morphine tolerance through a period of addiction and naloxone withdrawal therapy. Tolerance and physical dependence were induced by injecting the mice with morphine sulfate subcutaneously at 8-hour intervals, increasing the dose from 10 mg/kg BW every 24 h for 15 days. The animals were considered to be addicted when they were able to tolerate an otherwise lethal dose of 150 mg/kg 3 times a day. Results indicated that succinic dehydrogenase was inhibited throughout the 15-day period of morphine administration and that this effect was greatest in tolerant animals. Increasing the dose and duration of treatment did not cause further decreases in enzyme activity; instead, after 15 days levels of enzyme activity increased in addicted animals compared with tolerant mice. Furthermore, morphine abstinence for 2 days, markedly increased the levels of SD activity, while 6 days of abstinence had little effect. Naloxone withdrawal at each stage was associated with increased SD activity, but the increase was significant only in tolerant mice.
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PMID:Changes in succinic dehydrogenase activity in the central nervous system of mice during morphine dependence development, withdrawal and naloxone treatment. 404 Apr 49

The inner and outer membranes of Pasteurella haemolytica were separated by sucrose density gradient centrifugation after plasmolysis of the cells in 20% sucrose and fragmentation in a French pressure cell. Assays of the two membrane fractions for 2-keto-3-deoxyoctonate, succinate dehydrogenase, and NADH dehydrogenase and by sodium dodecyl sulfate-polyacrylamide gel electrophoresis indicated that each of the two membrane fractions was purified fivefold relative to the other. The outer membrane fraction contained two major proteins of molecular weights 30,000 and 42,000 (30K and 42K proteins), and the inner membrane fraction contained five proteins in approximately equal amounts. Intact bacteria as well as membrane fractions were extracted by procedures used by others for vaccine preparation to determine whether the outer membrane proteins were released. Extraction of the isolated membranes with 0.5 M potassium thiocyanate in 0.425 M NaCl with or without EDTA or with M sodium salicylate failed to release more than traces of the outer membrane proteins. Sodium dodecyl sulfate extracted essentially all of the proteins of both membranes, but the products of this procedure were of low solubility and presumably denatured. The inner membrane proteins were extracted with 0.5% Sarkosyl in 0.02 M sodium phosphate buffer (pH 7.5). The 42K outer membrane protein, most of the lipopolysaccharide, and some of the 30K outer membrane protein were extracted with 1% Zwittergent 3-16 in 0.25 M NaCl (pH 8), and the remaining 30K outer membrane protein was extracted with 1% deoxycholate in 0.25% NaCl (pH 8). Extraction of membranes in this sequence yielded partially purified membrane proteins that were soluble in dilute buffers.
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PMID:Identification and extraction of Pasteurella haemolytica membrane proteins. 620 95

The effects of zinc on the enzymes of hepatic mitochondria were investigated in rats that had been given zinc sulfate (10 mg Zn2+/100 g body wt) p.o. Administration of zinc caused a marked elevation of succinate dehydrogenase, glutamate dehydrogenase, cytochrome c oxidase and ATPase activities, whereas it did not cause significant changes in pyruvate carboxylase, malate dehydrogenase and isocitrate dehydrogenase activities. The effect of zinc as a function of time was greatest on succinate dehydrogenase. Zinc also produced a marked elevation of ATP concentration in the hepatic cytosol and a corresponding increase in ATPase activity in the hepatic mitochondria. Zinc content of the inner membrane of mitochondria was raised significantly by administration of zinc. The removal of zinc by washing in 10 mM EDTA caused a significant decrease of the increased succinate dehydrogenase activity caused by administration of zinc, while it did not lower ATPase activity. The addition of zinc in amounts of 10-10(3) ng Zn2+ per mg protein produced a significant increase in succinate dehydrogenase activity in the inner membrane of mitochondria, whereas ATPase activity was elevated significantly at 10(3)-10(4) ng Zn2+ per mg protein, indicating that zinc activated succinate dehydrogenase more sensitively than ATPase. The present investigation suggests that zinc taken up by hepatic mitochondria stimulates the electron transport system and oxidative phosphorylation and, as a result, increases the ATP concentration in the hepatic cytosol.
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PMID:Role of zinc as an activator of mitochondrial function in rat liver. 621 62

An improved method was developed to sequentially fractionate succinate-cytochrome c reductase into three reconstitutive active enzyme systems with good yield: pure succinate dehydrogenase, ubiquinone-binding protein fraction and a highly purified ubiquinol-cytochrome c reductase (cytochrome b-c1 III complex). An extensively dialyzed succinate-cytochrome c reductase was first separated into a succinae dehydrogenase fraction and the cytochrome b-c1 complex by alkali treatment. The resulting succinate dehydrogenase fraction was further purified to homogeneity by the treatment of butanol, calcium phosphate gel adsorption and ammonium sulfate fractionation under anaerobic condition in the presence of succinate and dithiothreitol. The cytochrome b-c1 complex was separated into chtochrome b-c1 III complex and ubiquinone-binding protein fractions by careful ammonium acetate fractionation in the presence of deoxycholate. The purified succinate dehydrogenase contained only two polypeptides with molecular weights of 70 000 anbd 27 000 as revealed by the sodium dodecyl sulfate polyacrylamide gel electrophoretic pattern. The enzyme has the reconstitutive activity and a low Km ferricyanide reductase activity of 85 mumol succinate oxidized per min per mg protein at 38 degrees C. Chemical composition analysis of cytochrome b-c1 III complex showed that the preparation was completely free of contamination of succinate dehydrogenase and ubiquinone-binding protein and was 30% more pure than the available preparation. When these three components were mixed in a proper ratio, a thenoyltrifluoroacetone- and antimycin A-sensitive succinate-cytochrome c reductase was reconstituted.
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PMID:Resolution and reconstitution of succinate-cytochrome c reductase: preparations and properties of high purity succinate dehydrogenase and ubiquinol-cytochrome c reductase. 624 48

Lactoperoxidase-catalyzed radioiodination was used to study the arrangement of the component peptides of succinate-cytochrome c reductase with respect to the aqueous phases on each side of the mitochondrial inner membrane. Mitochondria depleted of their outer membrane and inside-out vesicles purified from submitochondrial particles by the lectin-affinity procedure (D'Souza, M. P., and Lindsay, J. G. (1981) Biochim. Biophys. Acta 640, 463-472) were iodinated using immobilized preparations of lactoperoxidase. The labeled membranes were solubilized in detergent and the succinate-cytochrome c reductase was purified by immunoprecipitation with specific IgG. Analysis of the radioiodine distribution after sodium dodecyl sulfate-polyacrylamide gel electrophoresis and comparison with peptide stain patterns show that bands 2 (64 kilodaltons), 6 (30 kilodaltons), 9 (15 kilodaltons), and 11 (less than 10 kilodaltons) are labeled from the cytoplasmic surface of the membrane. Bands 1 (72 kilodaltons), 4 (48 kilodaltons), and 8 (20 kilodaltons) appear to be labeled on the matrix side of the membrane, while bands 3 (52 kilodaltons), 5 (35 kilodaltons), 7 (25 kilodaltons), and 10 (11 kilodaltons) are labeled from both sides of the membrane. Tentative identification of the labeled bands suggests that band 1 is the large subunit of succinate dehydrogenase. Bands 3 and 4 represent proteins which have been referred to as core proteins I and II. Bands 5 and 6 are the proteins associated with cytochromes b and c1, respectively; band 7 is the Rieske iron-sulfur protein.
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PMID:Labeling of succinate-cytochrome c reductase with 125I. Accessibility of the peptides to the aqueous phases on the cytosolic and matrix sides of the mitochondrial membrane. 628 97

A rapid and reproducible method has been developed for the simultaneous isolation of basolateral and brush-border membranes from the rabbit renal cortex. The basolateral membrane preparation was enriched 25-fold in (Na+ + K+)-ATPase and the brush-border membrane fraction was enriched 12-fold in alkaline phosphatase, whereas the amount of cross-contamination was low. Contamination of these preparations by mitochondria and lysosomes was minimal as indicated by the low specific activities of enzyme markers, i.e., succinate dehydrogenase and acid phosphatase. The basolateral fraction consisted of 35-50% sealed vesicles, as demonstrated by detergent (sodium dodecyl sulfate) activation of (Na+ + K+)-ATPase activity and [3H]ouabain binding. The sidedness of the basolateral membranes was estimated from the latency of ouabain-sensitive (Na+ + K+)-ATPase activity assayed in the presence of gramicidin, which renders the vesicles permeable to Na+ and K+. These studies suggest that nearly 90% of the vesicles are in a right-side-out orientation.
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PMID:Isolation of basolateral and brush-border membranes from the rabbit kidney cortex. Vesicle integrity and membrane sidedness of the basolateral fraction. 631 56

A tegumental fraction from fully developed larvae of Taenia taeniaeformis was recovered by low speed centrifugation following incubation of the parasites in a 0.1% solution of digitonin. Scanning electron microscopy of the parasite carcass revealed no surface microtrichs, and transmission electron microscopy indicated that the subtegumental layer was undamaged. The tegumental fraction, judging from the distribution of 3H-Concanavalin A, was enriched for surface components, exhibited low succinic dehydrogenase activity, and an electron microscopic examination of the pellet showed a slightly expanded but intact distal tegumental layer. The fraction, which made up 3.0% of the dry weight of the parasite, consisted of 52% protein and 32% lipid. Thirty-three proteins, ranging in Mr from 9,000 to 276,000 daltons, were detected after sodium dodecyl sulfate solubilization and polyacrylamide gel electrophoresis. Seven of these proteins were glycoproteins. Cholesterol, phosphatidylethanolamine, phosphatidylserine, and glycosphingolipids were the major lipids.
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PMID:Lipid and protein composition of the surface tegument from larvae of Taenia taeniaeformis. 647 Aug 83

Results from these studies demonstrate that we have purified a protein from rat prostate cytosol that is similar to the beta-protein (complex II) but different from the alpha-protein (complex I) reported by Liao et al. The purified receptor was different from androgen binding protein (ABP) in that ABP has a faster dissociation rate (6 min), a lower pI value (4.6), and requires higher concentrations of ammonium sulfate for precipitation (40-50%) than the prostatic androgen receptor. It is not likely that we have purified a serum sex-steroid binding protein since no such protein is found in rat serum. This report presents a rapid and efficient procedure for the purification of androgen receptor from rat ventral prostate. However, the present procedure only allowed us to obtain a limited quantity of purified receptor from each preparation. It is obvious that we need to scale up the purification of the receptor in order to study in detail its physicochemical properties and to produce monospecific antibodies against the protein. This work is in progress. In addition, we have demonstrated that two affinity labels can be used to bind covalently to the androgen receptor. Most importantly, these compounds can be used to characterize androgen receptors under both nondenaturing and denaturing conditions and represent useful tools for future work with androgen receptor proteins and androphilic proteins in general.
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PMID:Molecular properties of the androgen receptor in rat ventral prostate. 659 24

To determine whether certain outer membrane proteins are associated with growth of Bacteroides thetaiotaomicron on polysaccharides, we developed a procedure for separating outer membranes from inner membranes by sucrose density centrifugation. Cell extracts in 10% (wt/vol) sucrose-10 mM HEPES buffer (N-2-hydroxyethylpiperazine-N'-2-ethanesulfonic acid) (pH 7.4) were separated into two fractions on a two-step (37 and 70% [wt/vol]) sucrose gradient. These fractions were further resolved into outer membranes (p = 1.21 g/cm3) and inner membranes (p = 1.14 g/cm3) on sucrose gradients. About 20 to 26% of the total 3-hydroxy fatty acids from lipopolysaccharide and 2 to 3% of the total cellular succinate dehydrogenase activity were recovered in the outer membrane preparation. The inner membrane preparation contained 22 to 49% of the total succinate dehydrogenase activity and 2 to 3% of the total 3-hydroxy fatty acids from lipopolysaccharide. Outer membranes contained a lower concentration of protein (0.34 mg/mg [dry weight]) than did the inner membranes (0.68 mg/mg [dry weight]). Molecular weights of inner membrane polypeptides ranged from 11,000 to 133,000. The most prominent polypeptides had molecular weights ranging from 11,000 to 26,000. In contrast, the molecular weights of outer membrane polypeptides ranged from 17,000 to 117,000. The most prominent polypeptides had molecular weights ranging from 42,000 to 117,000. There were several polypeptides in the outer membranes of bacteria grown on polysaccharides (chondroitin sulfate, arabinogalactan, or polygalacturonic acid) which were not detected or were not as prominent in outer membranes of bacteria grown on monosaccharide components of these polysaccharides.
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PMID:Isolation and characterization of outer membranes of Bacteroides thetaiotaomicron grown on different carbohydrates. 671 79


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