Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:1.1.1.37 (malate dehydrogenase)
 4,591 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The reservoir animals, sandfly vectors and strains of Leishmania from foci in the southern region of Israel were studied. The rodent host species are: Psammomys obesus, Meriones crassus and probably Nesokia indica. The vector species are Phlebotomus papatasi, which were caught at all collecting sites and Ph. sergenti, which were collected in the area of the Dead Sea and in the Central Arava. Strains of Leishmania major isolated from rodents, vectors and man were serologically and enzymologically identical with regard to their excreted factor (EF) serotypes, their malate dehydrogenase (MDH), glucose-phosphate isomerase (GPI) and glucose-6-phosphate dehydrogenase (G6PDH) enzyme variant types, but exhibited three variant subtypes of 6-phosphogluconate dehydrogenase (6PGDH). The distribution of the 6PGDH subtypes correlates with three different geographical locations. Scarcity of water is the main factor limiting the biotopes of the sandflies and the spread of leishmaniasis. The subjects discussed are the dependence of sandfly distribution on rodent-burrow depth in arid areas and the inter-relationship between the leishmanial subtypes, vectors and hosts.
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PMID:Leishmaniasis in Israel: reservoir hosts, sandfly vectors and leishmanial strains in the Negev, Central Arava and along the Dead Sea. 638 58

The authors studied combined effect of aniline (20 mg/kg for a period of 4 weeks in drinking water) and nitrosodimethylamine (NDMA) (30 mg/kg, a single intragastric dose) on the activity of enzymes of different subcellular structures: endoplasmic reticulum (cytochromes P450, B5, acetylesterase), mitochondria (malate dehydrogenase) and the content of N-acetylneuraminic acid in rat liver and of lysosomes (beta-glucuronidase, beta-galactosidase). The combined action of NDMA and aniline was accompanied by more pronounced changes in the indices under investigation than isolated administration of the given chemical substances. The most pronounced aggravation of the unfavourable changes was observed in the activity of enzymes connected with the processes of oxidation and energy supply to the cell (malate dehydrogenase) and the metabolism of glucuronides (beta-glucuronidase) as well as in the content of N-acetylneuraminic acid. This may be connected with the modifying effect of aniline on the toxic effect of NDMA.
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PMID:Combined effect of nitrosodimethylamine and aniline on the enzyme systems of subcelluar structures. 680 54

Recently, it has been reported that paromomycin sulfate has marked anthelmintic efficacy against tapeworm infections in man. In the present study this drug was used in the treatment of 14 cases of diphyllobothriasis latum and 1 case of taeniasis saginata. Also, the actions of paromomycin sulfate on Diphyllobothrium ditremum and D. erinacei were examined pharmacologically using Magnus apparatus and biochemical methods. The results obtained were as follows. For the treatment, a total of 50 mg/kg of paromomycin sulfate divided into 2 doses was given orally at intervals of 30 minutes. Two hours after medication, 20 g of magnesium sulfate dissolved in 200--300 ml of water was given as purgative. One or 2 worms were found in the stools of 11 cases with D. latum and 1 case with T. saginata within 24 hours after medication, but scolex was found in only 2 of them. All cases were negative for the eggs or segments in stool examinations at 1 and 3 months after treatment. Except 1 case complained mild and transient vomiting no side effects were noticed. All cases showed no abnormality in blood examination, liver function test and urinalysis. Both of the proglottids of D. ditremum and D. erinacei showed muscle relaxation in Tyrode solution containing 10(-4) g/ml of paromomycin sulfate. In D. ditremum the recovery of muscle tonus was observed within 10--15 minutes after affection of this drug, while the persistence of muscle relaxation was seen in D. erinacei. The activity of phosphoglucose isomerase was slightly inhibited by 10(-3) M paromomycin sulfate while those of hexokinase, phosphofructokinase and glucose-6-phosphate dehydrogenase were not inhibited. In phosphoenolpyruvate-succinate pathway, the activity of fumarate reductase was slightly inhibited 10(-3) M paromomycin sulfate while those of phosphoenolpyruvate carboxykinase and malate dehydrogenase were not inhibited.
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PMID:[Efficacy of paromomycin sulfate against human cestodiasis and its pharmacological action on tapeworm in vitro]. 687 66

The previously isolated recessive mutant allele hex2-3 of Saccharomyces cerevisiae caused a defect in carbon catabolite repression of maltase, invertase, malate dehydrogenase, and respiration but at the same time led to an extreme sensitivity to maltose (Zimmerman and Scheel, 1977; Entian and Zimmermann, 1980). Addition of maltose to a growing culture of a hex2-3 mutant resulted within 60 to 90 min in an inhibition of growth, glycolysis, and de novo protein synthesis. This was not accompanied by any abnormal levels of glycolysis metabolites or glycolytic enzyme activities. However, inhibitory effects coincided with a dramatic increase in intracellular glucose up to 150 mM relative to cell water as opposed to 2.5 mM in wild-type cells. This abnormal behavior is interpreted as a result of an uncontrolled maltose uptake in hex2 mutants, which in combination with increasing maltase activity results in an accumulation of intracellular glucose. Obviously the amount of available glucose surpassed glycolytic capacity in hex2 mutants. Properties of mutant alleles hex2 and hex1 (see Entian and Zimmermann, 1980) clearly show, that specific gene functions are involved in adapting the rate of sugar uptake into the cell to the actual glycolytic capacity.
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PMID:A defect in carbon catabolite repression associated with uncontrollable and excessive maltose uptake. 700 23

Brine shrimp nauplii challenged with artificial sea water containing 2.5 M NaCl maintain significantly higher levels of cytoplasmic malate dehydrogenase (s-MDH) than larvae incubated in sea water having 0.5 M NaCl. Eight to ten hours after emergence, free-swimming nauplii living in 0.5 M NaCl exhibit a steady decline of s-MDH for 20-40 hours; the decreased is less and stabilizes earlier-in nauplii incubated in 2.5 M NaCl. The 14C-labeled amino acids produced by H 14CO3 fixation were rapidly incorporated into newly formed s-MDH protein as assayed using quantitative rocket immunoelectrophoresis (IEP) with monospecific antiserum prepared against purified brine shrimp s-MDH. Higher rates of enzyme biosynthesis ( greater than 45%) occurred in 2.5 M NaCl together with rapid s-MDH turnover (half-life = 17 hours), accounting for the difference observed in enzyme level between different salt regimes. In contrast, incorporation of 14C-labeled amino acids into total cytoplasmic protein decreased slightly in high salt, suggesting that a preferential synthesis of s-MDH is taking place. Temporal patterns of s-MDH during embryonic development were monitored using both catalytic activity and quantitative IEP assays. Levels of s-MDH seen in encysted gastrulae (0.22 units or 0.57 microgram s-MDH protein/100 embryos) remain relatively constant through the E1 and E2 emergent stages until the exhibited decline observed in the naupliar stage. The results are discussed in relation to the bioenergetics and temporal development of water and electrolyte regulation in nauplii.
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PMID:Larval brine shrimp malate dehydrogenase: biosynthesis and temporal pattern related to environmental salinity. 707 58

Studies on dehydrogenase enzyme inhibition have been extended with the design, synthesis, and correlation analysis of 7-[(substituted-benzyl)oxy]-, 7-[(substituted-phenethyl)oxy]-, and 7([substituted-phenoxy)ethoxy]-4-hydroxyquinoline-3-carboxylic acids. Sixteen new congeners and the fifteen molecules previously synthesized have been tested against cytoplasmic malate dehydrogenase and lactate dehydrogenase, as well as against mitochondrial malate dehydrogenase. The lipophilic congeners show a clear specificity for inhibition of the mitochondrial enzyme. Correlation analysis of the data on the three enzymes allows a comparison of the binding sites in quantitative terms, while examination of the data on inhibition of ascites tumor cell respiration affords an indication of membrane transport. A newly developed high-pressure liquid chromatography based retention index is compared to the octanol-water pi constant as a model for hydrophobic interactions.
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PMID:4-hydroxyquinoline-3-carboxylic acids as inhibitors of cell respiration. 2. Quantitative structure-activity relationship of dehydrogenase enzyme and Ehrlich ascites tumor cell inhibitions. 708 23

Malate dehydrogenase from the organism Halobacterium marismortui was studied in solutions of varying salt concentration by using a small-angle X-ray system employing a linear position sensitive detector. Considerations pertaining to the study of absorbing multicomponent solutions are presented. The radius of gyration of halophilic malate dehydrogenase was found to be 31.8 +/- 0.6 A and the shape of the molecule spheroidal. The scattering from prolate ellipsoids of eccentricity between 1 and 2 best fitted the data while for oblate ellipsoids the scattering was best fitted for eccentricities between 1 and 0.5. No significant change in the radius of gyration or anisotropy of halophilic malate dehydrogenase was found in the range of NaCl concentrations studied (1-4 M). The contrast matching electron density was found to be 0.407 +/- 0.002 e/A3. A parallel study of bovine serum albumin yielded within experimental error a similar contrast matching electron density of 0.404 +/- 0.006 e/A3. This information combined with the diffusion coefficient and the amount of water and salt associated with halophilic malate dehydrogenase renders the existence of an outer hydration shell unlikely. The data are rather consistent at low resolution with a spheroidal particle of uniform electron density.
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PMID:Small-angle x-ray scattering study of halophilic malate dehydrogenase. 717 47

Exposure to simulated weightlessness (7-day water immersion and 7-day head-down tilt) caused a decrease in the activity of malate (MDH) and isocitrate dehydrogenase (ICDH), and creatine phosphokinase dehydrogenase (ICDH), and creatine phosphokinase (CPK) at the expense of its MM isoform whereas the activity of alanine (ALT) and aspartate aminotransferase (AST) and pattern of distribution of MDH isoforms remained unchanged. Exposure to acceleration of +3 Gz before and after simulated weightlessness revealed similar changes in the activity of MDH, ICDH, ALT, AST and MDH cytoplasmic fractions. However, the higher increase in the enzyme activity after simulated weightlessness may give evidence for a greater change in cell membrane permeability during acceleration effects that followed simulated weightlessness.
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PMID:[Energy-metabolism enzymes during combined exposure of the body to simulated weightlessness and gravitational overloads]. 728 61

Large-scale growth of extreme halophilic bacteria from the Dead Sea and purification of malate dehydrogenase (and other proteins) in quantities of hundreds of milligrams makes possible a detailed study of the adaptation to high salt. Halophilic malate dehydrogenase is stable at 20 degrees C in NaCl solutions between 2.5--5 M. Below 2.5 M NaCl time-dependent inactivation, paralleled by structural changes, sets in. Within the time scale of the sedimentation, diffusion and circular dichroism experiments discussed here, it was possible to analyze data corresponding to the active halophilic malate dehydrogenase between 1 M and 5 M NaCl. The striking observation was that rather minor conformation changes were observed over the whole range, yet the special properties of the halophilic enzyme seem to be related to its capacity of associating with unusually large amounts of water and of salts, quite distinct from non-halophilic counterparts. These special properties seem to be related to the intact structure of the protein. Some parallel properties of halophilic glutamate dehydrogenase are also discussed.
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PMID:Structure and activity of malate dehydrogenase from the extreme halophilic bacteria of the Dead Sea. 1. Conformation and interaction with water and salt between 5 M and 1 M NaCl concentration. 729 56

The stability of halophilic malate dehydrogenase increases with increasing salt concentration and with decrease in temperature. Stabilization by various salts, at high salt concentrations, follows the Hofmeister series. The enzyme inactivation rates closely match dissociation of the dimeric enzymes into monomeric subunits and unfolding of the polypeptide chains, as followed by velocity sedimentation, light scattering and circular dichroism measurements. The alpha-helix content goes to zero upon denaturation. Unusual water and salt binding properties of the native enzyme (cf. preceding paper, in this journal) are believed to be largely lost upon enzyme dissociation and unfolding. The properties thus seem to be associated with the intact structure of the enzyme.
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PMID:Structure and activity of malate dehydrogenase from the extreme halophilic bacteria of the Dead Sea. 2. Inactivation, dissociation and unfolding at NaCl concentrations below 2 M. Salt, salt concentration and temperature dependence of enzyme stability. 729 57


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