Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:1.6.99.3 (diaphorase)
 5,903 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Biochemical alterations in guinea pig lungs caused by hematite dust were followed at 150 days after intratracheal administration of the dust. In vivo dust exposure caused a significant increase in mitochondrial protein content and cytochrome c oxidase activity whereas diaphorase activity remained unaltered. Mitochondria from the exposed animals were apparently in a swollen state and their contraction profile upon the addition of ATP reflected permeability changes. However, in vitro dust caused no significant alterations. Significant increases in glycogen content along with an insignificant decrease in glycogen phosphorylase activity were also observed in hematite-treated guinea pig lungs. Decrease in drug-metabolizing enzymes such as aniline hydroxylase and tyrosine aminotransferase activities were also evident in the postmitochondrial fraction of the siderotic lungs. [3H]Leucine-incorporation studies showed increased protein synthesis in the postmitochondrial fraction. Increase in protein synthesis in mitochondria was only marginal whereas in whole homogenate it decreased considerably. Experiments employing dust tagged with radioactive iron indicated the rapid mobilization of iron from lung and its distribution to various organs. The presence of iron-binding protein was confirmed by employing Sephadex gel-filtration techniques.
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PMID:Biochemical studies on the toxicity of hematite dust. 664 70

Intraperitoneal administration of 150 mg dexamethasone (DEX) Kg-1 body wt for four days to rhesus monkeys resulted in statistically significant increases in the activities of hepatic tyrosine aminotransferase (3 fold), microsomal cytochrome P450 (2 fold) and erythromycin N-demethylase (4 fold), but no change in the activities of aminopyrine N-demethylase and NADPH cytochrome c reductase. Three peaks were obtained from control or DEX-treated monkey livers on fractionation of detergent solubilized microsomes by anion exchange chromatography on DE-52. Peak II obtained from DEX-treated monkey microsomes on DE-52 demonstrated the highest specific activity of cytochrome P450 (5.84 nmol mg-1 protein) as compared to other peaks from the same microsomes or any of the peaks obtained from the control microsomes. Sodium dodecyl sulfate polyacrylamide gel electrophoresis of the microsomes from control and experimental animals and peak II obtained after anion exchange chromatography of DEX-treated microsomes demonstrated the intensification of two polypeptides of 52.5 and 50 kDa. The results indicate that DEX is an inducer of cytochrome P450 and dependent erythromycin N-demethylase in non-human primate, Macaca mulatta.
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PMID:Induction of hepatic microsomal cytochrome P450 by dexamethasone in rhesus monkey (Macaca mulatta). 780 39

Epimastigotes of Trypanosoma cruzi, the causative agent of Chagas disease, catabolize proteins and amino acids with production of MH3, and glucose with production of reduced catabolites, chiefly succinate and L-alanine, even under aerobic conditions. This "aerobic fermentation of glucose" is probably due to both the presence of low levels of some cytochromes, causing a relative inefficiency of the respiratory chain for NADH, reoxidation during active glucose catabolism, and the lack of NADH dehydrogenase and phosphorylation site I, resulting in the entry of reduction equivalents into the chain mostly as succinate. Phosphoenol pyruvate carboxykinase and pyruvate kinase may play an essential role in diverting glucose carbon to succinate or L-alanine, and L-malate seems to be the major metabolite for the transport of glucose carbon and reduction equivalents between glycosome and mitochondrion. The parasite contains proteinase and peptidase activities. The major lysosomal cysteine proteinase, cruzipain, has been characterized in considerable detail, and might be involved in the host/parasite relationship, in addition to its obvious role in parasite nutrition. Among the enzymes of amino acid catabolism, two glutamate dehydrogenases (one NADP- and the other NAD-linked), alanine aminotransferase, and the major enzymes of aromatic amino acid catabolism (tyrosine aminotransferase and aromatic alpha-hydroxy acid dehydrogenase), have been characterized and proposed to be involved in the reoxidation of glycolytic NADH.
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PMID:Intermediate metabolism in Trypanosoma cruzi. 805 82