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)

Thioacetamide (100 mg/kg), when administered to normal rats, caused a significant increase in the activities of 5'-nucleotidase and gamma-glutamyl transpeptidase and a decrease in the activities of glucose 6-phosphatase and succinate dehydrogenase enzymes in the liver. DNA, RNA, and proteins were increased while the cytochrome P450 in the microsomal fraction and the glycogen content in the liver were decreased significantly. Elevations in the activities of GOT, GPT, and alkaline phosphatase and bilirubin content in serum were also observed. Picroliv, a standardised glycoside fraction of Picrorhiza kurroa, in doses of 12.5 and 25 mg/kg prevented most of the biochemical changes induced by thioacetamide in liver and serum. The hepatoprotective activity of Picroliv was comparable with that of silymarin, a known hepatoprotective agent obtained from seeds of Silybum marianum.
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PMID:Picroliv affords protection against thioacetamide-induced hepatic damage in rats. 206 53

A (H+ + K+)-ATPase-enriched membrane fraction derived from the fundic portion of hog gastric mucosa was obtained by a combination of differential and repeated 7% Ficoll gradient centrifugation. The microsomal membrane fraction isolated by repeated 7% Ficoll gradient centrifugation was free of ouabain-sensitive (Na+ + K+)-ATPase, 5'-nucleotidase and succinate dehydrogenase; and it was highly enriched in (H+ + K+)-ATPase and K(+)-stimulated p-nitrophenylphosphatase (p-NPPase). The (H+ + K+)-ATPase had a pH optimum of 7.4 and was stimulated by Tl+, K+, Rb+ and NH4+ with Ka values of 0.0667, 0.526, 0.667 and 3.03 mM, respectively, at this pH. On the other hand, monovalent cations such as Na+, Li+ and (CH3)4N+ as well as divalent cations such as Cu2+, Ca2+, Ba2+, Sr2+ and Cd2+ inhibited this enzyme activity concentration-dependently. Ouabain and oligomycin had no effect, whereas omeprazole, a specific (H+ + K+)-ATPase inhibitor, inhibited this enzyme activity in a pH-dependent manner. Sodium dodecyl sulfate (SDS)-polyacrylamide gel electrophoresis showed a major band (greater than or equal to 90% of protein) at 97,400 daltons, which was phosphorylated in the presence of Mg2+ and [gamma-32P]-ATP and dephosphorylated in the presence of K+. The present method was very simple, and the (H+ + K+)-ATPase activity of the microsomal fraction obtained by this method was much higher compared with those obtained by other methods such as free-flow electrophoresis.
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PMID:Purification and characterization of (H+ + K+)-ATPase from hog gastric mucosa. 215 97

Merocyanine 540 (MC 540) is a photosensitizing dye that is used clinically for the purging of autologous bone marrow grafts and preclinically for the inactivation of enveloped viruses in blood products. Its mechanism of action is not yet well understood. This paper investigates the sites of MC 540-mediated photodamages in L1210 leukemia cells by examining the effects of MC 540-sensitized photoirradiation on several soluble and membrane-bound marker enzymes. When exposed to MC 540 and white light under a standard set of conditions, the activities of Na+/K(+)-ATPase, Mg2(+)-ATPase, and 5'-nucleotidase (three plasma membrane-bound enzymes) were reduced by 54, 49, and 55%, respectively. None of the intracellular enzymes included in this survey was affected by MC 540-sensitized photoirradiation as long as the plasma membrane remained intact. The two soluble enzymes, lactate dehydrogenase and malate dehydrogenase, remained refractory to MC 540-sensitized photoirradiation even after the plasma membrane had been disrupted. By contrast, the activities of the membrane-bound enzymes, NADPH-cytochrome c reductase and succinate dehydrogenase, were reduced in cell lysates by 55 and 81%, respectively. Purified NADPH-cytochrome c reductase was about 3 times less sensitive than the microsomal enzyme, suggesting that the membrane environment facilitated photoinactivation. The MC 540-sensitized photoinactivation of enzymes was accelerated in the presence of deuterium oxide and inhibited if oxygen in the medium was displaced by nitrogen or azide was added to the medium. Taken together, these data support the view that the plasma membrane is a major target of MC 540-mediated photodamages, that the inactivation of membrane-bound enzymes is an oxidative process, and that at least some photodynamic damages are mediated by type II chemistry.
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PMID:Merocyanine 540-sensitized photoinactivation of soluble and membrane-bound enzymes in L1210 leukemia cells. 217 31

We report here the isolation of fractions enriched in components of the myelin-like membranes surrounding the giant axons of the earthworm. Lumbricus terrestris L. The composition and purity of the fractions have been assessed using SDS-protein electrophoresis, Western immunoblots, and electron microscopy. Preliminary enzyme assays indicated that the mitochondrial marker, succinate dehydrogenase, has a similar specific activity distribution in earthworm nerve cord and in mouse liver sedimentation velocity fractions, however, the distribution of the total units of activity among the fractions seems to indicate the existence of smaller mitochondria in earthworm nerve cord compared with mouse liver mitochondria. In earthworm nerve cord fractions, Na+/K+ ATPase and Ca2+/Mg2+ ATPase were found to be enriched exclusively in the fraction containing large plasma and myelin-like membranes, while in the mouse liver fractions, the total units of these two enzymes were found to be distributed broadly among fractions. 5'-Nucleotidase activity in the earthworm nerve cord seemed to be restricted to the microsomal fractions (endomembrane network), with a very low activity associated with the large plasma and myelin-like membrane fraction. We have established the presence of keratins or prekeratins in the myelin-like membranes, probably in the form of tonofilaments. However, we could not show that the desmosome-like structures, characteristic of these membranes, are composed of those proteins described for vertebrate epithelial desmosomes.
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PMID:Isolation and initial characterization of myelin-like membrane fractions from the nerve cord of earthworms (Lumbricus terrestris L). 246

The zonal distribution of enzyme activities was measured by quantitative cytochemistry in cryosections of liver from three normal children and five infants with idiopathic hepatitis of infancy. Optimal conditions for cytochemical reactions were first validated in rat liver and subsequently used in human livers to quantify zonal activities of acid phosphatase (AP), succinate dehydrogenase (SDH), glutamate dehydrogenase (GDH), glucose-6-phosphatase (G6P) and NADPH-dehydrogenase (ND). In normal rat and human livers, activities were greater for SDH and G6P in periportal and for GDH and ND in perivenular hepatocytes, while AP was evenly distributed along the sinusoids. In five infants with idiopathic hepatitis of infancy (IHI), a similar trend of distribution was observed for the two mitochondrial (SDH and GDH) and the two microsomal (G6P and ND) enzymes, although the distribution gradient was less pronounced than, in normal livers. AP showed a mildly greater periportal than perivenular activity. This preliminary study shows that a similar metabolic zonation exists for these enzymes in human livers as is observed in rats.
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PMID:The application of quantitative cytochemistry to study the acinar distribution of enzymatic activities in human liver biopsy sections. 254 21

Binding of [3H]Ro5-4864, a specific ligand for "peripheral type" benzodiazepine receptors, was determined in subcellular fractions of guinea pig lung. Even though the level of binding was predominant in the mitochondrial fraction, nuclear and cytosolic fractions also contained significantly measurable amounts of binding sites. The presence of binding sites in the microsomal fraction and in a fraction intermediate in density between the mitochondria and microsomes depended on which buffer was used to homogenize the tissue. If calcium-containing mannitol buffer was used, binding was negligible in the postmitochondrial organelles. However, in the case of sucrose buffer which did not contain any calcium, the postmitochondrial organelle fractions contained measurable amounts of binding sites. Most probably, these binding sites were of mitochondrial and nuclear origin. Furthermore, binding sites in the mitochondria were associated with the succinic dehydrogenase-enriched mitochondrial inner membrane, but not with the monoamine oxidase- and cholinephosphotransferase-enriched outer mitochondrial membrane. Furthermore, several proteolytic enzymes caused a decrease in binding of the ligand to the mitochondrial membrane only under hypotonic conditions and not under isotonic conditions, suggesting that the location of the receptors is inside the mitochondria.
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PMID:Subcellular distribution of "peripheral type" binding sites for [3H]Ro5-4864 in guinea pig lung. Localization to the mitochondrial inner membrane. 255 Apr 54

The subcellular distribution patterns of aromatase, 5 alpha- and 5 beta-reductase in the hypothalamus/preoptic area of Japanese quail were studied using standard methods of centrifugation, and fractional constituents were identified by marker enzymes. Aromatase was concentrated 8-fold in the 100,000 g pellet (P3) along with a 3-fold enrichment in the microsomal marker NADPH-cytochrome c reductase (NCR) a result consistent with glandular tissues. In addition, aromatase was enriched 2-fold in the 11,000 g pellet (P2) and, owing to its large size, this fraction accounted for more total activity than P3. Although P2 contained the mitochondrial marker succinate dehydrogenase (SDH), treatment with Triton X-100 to solubilize membranes and release occluded enzymes increased measured NCR and the cytosol marker lactate dehydrogenase (LDH) 2- and 4-fold, respectively--evidence that this fraction was composed of mitochondria plus synaptosomes (pinched-off nerve terminals). To further explore the location of aromatase in the 11,000 g fraction, P2 was exposed to hypotonic buffer, a treatment known to cause lysis of synaptosomes, and then separated into three fractions P2a (11,000 g pellet), P2b (100,000 g pellet) and P2s (100,000 g supernatant). Aromatase colocalized with the microsomal marker NCR (13- and 4-fold increase, respectively) in the 100,000 g (P2b) pellet which was, however, devoid of mitochondrial enzyme activity. We infer from this that a significant portion of aromatase in brain is associated with smooth membranes present inside synaptosomes. 5 beta-Reductase in quail brain subfractions was enriched 6-fold in the 100,000 g supernatant together with a 4-fold enrichment in the cytosolic marker LDH.(ABSTRACT TRUNCATED AT 250 WORDS)
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PMID:Localization of aromatase in synaptosomal and microsomal subfractions of quail (Coturnix coturnix japonica) brain. 271 59

Young adult rats absorbed 50 p.p.m. Cd2+ added to drinking water. After 6 weeks, 3, 6 and 9 months of treatment, the ultrastructural condition of liver, kidney and muscle was observed by electron microscopy. The choice of these tissues was determined by their differences in the capacity to accumulate Cd2+: the liver is able to concentrate a considerable amount of metal, but redistributes it throughout the entire organism, while the kidney collects it in view of its elimination. Muscle contains the least Cd2+. A general regression in mitochondria cristae accompanied by a vesiculation and a fragmentation of endoplasmic reticulum appeared simultaneously in the three tissues, at as early as 6 weeks of treatment, and extended progressively with its continuation supporting evidence of a general attack of the intracellular membrane systems. Cd2+ stimulation of membrane-degrading enzymes such as phospholipases and proteases was suggested. A concomitant diminution in glycogen stores was noted. Active synthesis of neutral lipids, especially cholesterol esters, took place in liver mitochondria of treated rats in collaboration with rough endoplasmic reticulum, and progressively generated a multiplication of electron-transparent inclusions in cytoplasm. Isolated mitochondria from liver, kidney and muscle of Cd2+-treated rats maintained partial energy coupling, but displayed a rapid early fall in cytochrome oxidase followed by a partial restoration after 6 months of treatment, and a progressively slackening of succinate dehydrogenase. Isolated vesicles of liver mitochondria inner membrane of treated rats behaved as intact mitochondria, indicating changes inside the membrane itself. Addition in vitro of the metal ion to mitochondria and also to inner membrane vesicles isolated from control rats revealed that Cd2+ was able to stop completely succinate dehydrogenase, but was totally ineffective on cytochrome oxidase. Membrane fixation of Cd2+ on the flavoprotein or SH associated with succinate dehydrogenase is proposed. Considering the close parallelism of the extensive depression of microsomal NADPH cytochrome c reductase and the rapid fall in mitochondrial cytochrome oxidase, it is suggested that an indirect inhibition process occurs, through Cd2+-induced diminution of a constituent common to all cytochromes in the cell.
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PMID:Mitochondria alterations in Cd2+-treated rats: general regression of inner membrane cristae and electron transport impairment. 293 99

Alkaline phosphatase was released from protoplasts of the yeast Saccharomyces cerevisiae without cell lysis not only by phosphatidylinositol (PI)-specific phospholipase C but also by phosphatidylcholine (PC)-hydrolyzing phospholipase C. Activities of mitochondrial enzymes such as succinate dehydrogenase, antimycin-sensitive NADH-cytochrome c reductase, and oligomycin-sensitive ATPase were decreased by the action of PC-hydrolyzing phospholipase C. Hydrolysis of microsomal PC or PI did not cause any decrease in the activities of NADPH-cytochrome c reductase and antimycin-insensitive NADPH-cytochrome c reductase. In the requirement of phospholipids, the properties of yeast mitochondrial enzymes were very close to those of mammalian mitochondrial enzymes, whereas those of yeast microsomal enzymes were completely different from those of mammalian microsomal enzymes.
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PMID:Effects of phospholipases C on membrane-bound enzymes of yeast. 296 99

Studies have been made on the activity of cation- and anion-stimulated ATPases, as well as succinic dehydrogenase in homogenates and subcellular fractions from osmoregulatory organs of marine (elasmobranch and teleost) and freshwater (teleost) fishes, amphibians, reptiles, birds and mammals. The activity of Na+, K+-ATPase was found to be rather similar in almost all osmoregulatory organs of the species investigated. The highest level of Cl-stimulated ATPase was found in microsomal fraction of the kidneys from birds and mammals. Succinic dehydrogenase activity is significantly higher in the renal tissue of mammals, both in total homogenates and in mitochondrial fraction.
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PMID:[Adenosine triphosphatase activity in the osmoregulatory organs of vertebrates]. 301 7


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