Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:3.1.3.9 (glucose-6-phosphatase)
 3,081 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

An improved method has been developed for the assay of hexokinase (EC 2.7.1.1) levels in human tissue homogenates. The enzyme is quantitated by the spectrophotometric measurement, at 340 nm, of NADPH formed according to the reaction scheme: [formula: see text] In tissue homogenates a number of enzymes are present which can interfere with the assay by reacting with substrates or products of the assay reactions. In the described procedure hexokinase is assayed directly in homogenates under conditions in which the effect of possible contaminating enzymes (glucose dehydrogenase, EC 1.1.1.47; glucose 6-phosphatase, EC 3.1.3.9; glucose phosphate isomerase, EC 5.3.1.9; 6-phosphogluconate dehydrogenase EC 1.1.1.44; and NADP-reducing enzymes) are eliminated. Precision studies on the assay gave within-day reproducibility of 4.3% (CV) on a tissue having a mean activity of 1.68 U/g of tissue, and day-to-day variability of 15% (CV) for a tissue averaging 1.83 U/g of tissue.
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PMID:An improved assay for hexokinase activity in human tissue homogenates. 976 31

The importance of the glycolytic flux for the success of Biomphalaria-Schistosome sporocyst interaction was acertained in this study. Hexokinase (HK), pyruvate kinase(PK), glucose phosphate isomerase(GPI) and lactate dehydrogenase (LD) as four important glycolytic enzymes were markedly stimulated in trematode infected Biomphalaria alexandrina when measured two weeks post exposure to infection with Schistosoma mansoni miracidia. On the other hand phosphoenolpyruvate carboxy kinase (PEPCK), glucose-6-phosphatase (G6Pase) and fructose 1,6 diphosphatase(FDPase) as three gluconeogenic enzymes were slightly affected which confirm the importance of the glycolytic pathway for schistosome-exposed snails. Effect of LC25 of Solanum nigrum leaves dry powder as plant molluscicide on HK, PK and GPI were tested. Treatment with this plant resulted in a significant inhibition of these three investigated enzymes. LC10 concentrations of S. nigrum reduced considerably the infection rate of B. alexandrina with S. mansoni to be 34% compared to an infection rate of 80% in control, non-treated snails. Longer prepatent period and remarkable decrease in cercarial production was also recorded in snails treated with the sublethal concentrations of the molluscicide. As conclusion, susceptibility of B. alexandrina to infection with the digenetic trematode S. mansoni is correlated to the activity levels of the glycolytic enzymes. Moreover, sublethal and less pollutant concentration of S. nigrum could be recommended to control schistosomiasis by disturbing the intramolluscan environment of the parasite.
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PMID:Susceptibility of Biomphalaria alexandrina to infection with Schistosoma mansoni: correlation with the activity of certain glycolytic enzymes. 1094 15

Effect of Capparis spinosa (C. spinosa) and Acacia arabica (A. arabica) dry powder as plant molluscicide on some glycolytic and gluconeogenic enzymes on snail tissues, was investigated. Lactate debydrogenase (LDH), Pyruvate Kinase (PK), Hexokinase (HK), phosphofructokinase (PFK), glucose phosphate isomerase (GPI) as important glycolytic enzymes, were markedly manipulated by both plants when measured one day and one week post-treatment. On the other hand glucose-6-phosphatase (G-6Pase), fructose 1.6 diphosphatase (FDpase), phosphoenol pyruvate carboxykinase (PEPCK) as gluconeogenic enzymes were significantly affected by the moluscicidal plants. In addition, some other parameters as glycogen, glucose, total protein, 5-nucleotidase alpha-hydroxybutyrate dehydrogenase (HBDH) and succinate dehydrogenase (SDH) as kreb's cycle enzyme were tested. As conclusion, LC25 and LC50 concentrations of C. spinosa and A. arabica might render B. alexandrina physiologically unsuitable for S. mansoni infection.
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PMID:Induced changes in biochemical parameters of the molluscan tissues non-infected using two potent plants molluscicides. 1528 76