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)

Enzyme binding studies have been conducted on several reduced nicotinamide adenine dinucleotide analogues having different substitutions at the 8 position of the adenine. The following analogues were synthesized for this study: 8-bromo-, 8-(methylamino)-, 8-(dimethylamino)-, and 8-(ethylamino)-substituted NADH. The conformation of these analogues was also studied. 1H and 13C nuclear magnetic resonance analysis showed that there was rotation about the adenine glycosyl bond and that the rotational preference depended on the C8 substituent. The bromo and dimethylamino analogues were predominantly in the syn conformation, while the anti conformation prevailed in the other derivatives as it does in the native NADH. Use of these analogues as co-enzymes by Pseudomonas aeruginosa transhydrogenase, Beneckea harveyi FMN:NADH oxidoreductase, rabbit muscle lactate dehydrogenase, beef heart lactate dehydrogenase, horse liver alcohol dehydrogenase, and yeast alcohol dehydrogenase resulted in enzyme activity in all cases. The bromo and dimethylamino analogues were bound significantly tighter than the other analogues for at least two of the enzymes studied. The data are discussed with respect to the ability of these enzymes to bind nucleotides which are in the syn conformation.
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PMID:Reduced nicotinamide 8-(alkylamino)adenine dinucleotides: enzyme-coenzyme interactions with different adenyl glycosyl bond conformations. 677 54

The maximal rate of some cerebral enzymatic activities related to energy transduction (hexokinase; phosphofructokinase; lactate dehydrogenase; citrate synthase; malate dehydrogenase; total NADH-cytochrome c reductase; cytochrome oxidase), amino acid metabolism (glutamate decarboxylase; glutamate dehydrogenase) and cholinergic metabolism (acetylcholine esterase) were tested in the cerebral cortex and in sub-cortical area of rats. The evaluations were performed both in the homogenate in toto and in the crude mitochondrial fraction, before and after a postdecapitative normothermic ischemia of 5, 10, 20, and 40 min duration. The results are discussed also with respect to the pharmacological pretreatment with two biological substances which may modulate amino acid (L-alanine) and phospholipid metabolism (CDP-choline). The analysis of the present data suggests the occurrence in brain tissue of a variety of interrelated factors implicated in the ischemia-induced changes of the maximal rate of the enzymatic activities related to the energy transduction. These include: (a) rearrangement of the enzymatic activities because of the changed metabolic and chemico-physical condition; (b) decrease in the activity of enzymes related to the electron transfer chain and glycolysis; (c) changes in enzymes related to mitochondrial membranes. The effects of in vivo administration of alanine or CDP-choline, even if significant, are not consistent throughout the time period studied.
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PMID:Changes induced by ischemia on some cerebral enzymatic activities related to energy transduction and amino acid metabolism. 685 30

Parallel stereo- and cytospectrophotometric examinations of human myocardial capillaries, 20-60 min after biological death were carried out. The activity of alkaline phosphatase, adenosine triphosphatase, lactate dehydrogenase and NAD-diaphorase in the capillary wall in relation to the sex and age in cardiovascular pathology, renal diseases and leukemias were studied. The permeability and level of energy supply of transendothelial transport were found to depend on the kind of the main pathological process and type of death. According to the parameters under study, the functional state of the capillary network of the myocardium in atherosclerosis with or without its combination with hypertension and also in secondary renal hypertension is described.
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PMID:[Stereological characteristics and enzymatic activity of myocardial capillaries in different variants of pathology and death (data from immediate autopsies)]. 686 Jan 68

In this simple and direct method for determining total bile acids in serum, the serum was mixed with sodium pyruvate, a lactate dehydrogenase blocker, and bile acids were then measured spectrophotometrically after the following enzyme reaction. Bile acids are converted to 3-oxo bile acids with 3 alpha-hydroxysteroid dehydrogenase (EC 1.1.1.50) with concomitant reduction of NAD+ to NADH. The hydrogen in the NADH generated is transferred by diaphorase (EC 1.6.4.3) to nitrotetrazolium blue to yield diformazan 540 nm). Analytical recovery of the various bile acids in serum averaged 96.2%. The CV for the day-to-day variation was 4.3%. Normal values are less than 7 mumol/L. Total serum bile acids were estimated by this method in 118 fasting patients with various liver diseases. This determination is clearly shown to be useful as a liver-function test.
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PMID:Direct spectrophotometry of total bile acids in serum. 689 53

Androgen level and the activity of lactate dehydrogenase, succinic dehydrogenase, 17 beta-hydroxysteroid dehydrogenase and NADP-diaphorase was studied in cultured Leydig cells obtained from testes of male mice from inbred strains KP and CBA following a single injection of cadmium chloride. Mice from CBA strain, known to be resistant to the toxic effects of cadmium showed no differences in the enzyme activity and endocrine function of gonads, as compared with control animals. In KP mice, sensitive to cadmium, a marked decrease of activity of all studied dehydrogenases, as well as a fall of androgen level was observed following cadmium administration. The decrease of hormone secretion occurred on the 2nd day of tissue culture and showed a correlation with the 17 beta-hydroxysteroid dehydrogenase activity.
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PMID:Effect of cadmium on androgen level and oxidoreductive enzymes activity in cultured leydig cells of KP and CBA mice. 694 54

The energy metabolism of the English E-CMO strain of contagious equine metritis bacterium was studied in whole cells and cell extracts. This bacterium appears to have an active Krebs cycle and probably obtains energy by oxidative phosphorylation since glycolysis and the hexose monophosphate pathways appear to be absent. These conclusions are based on the findings that [U-14C]glucose incorporation by this bacterium is below the level of detection, and that respiration is stimulated by Krebs cycle intermediates (i.e., malate, citrate, and succinate), but not by glucose, fructose, maltose, or sucrose. Furthermore, support comes from the fact that enzymes generally associated with the Krebs cycle and electron transport (i.e., malate dehydrogenase, succinate dehydrogenase, isocitrate dehydrogenase, fumarate hydratase, malate dehydrogenase [decarboxylating], cytochrome oxidase, superoxide dismutase, NADH dehydrogenase, and catalase) were detected. Those enzymes normally associated with glycolysis and the hexose monophosphate pathways (i.e., hexokinase, glucose 6-phosphate dehydrogenase, fructose biphosphate aldolase, glycerol 3-phosphate dehydrogenase, phosphoenolpyruvate carboxykinase, pyruvate kinase, phosphate acetyl transferase, acetate kinase, alcohol dehydrogenase, and lactate dehydrogenase) were below the level of detection.
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PMID:Energy metabolism of the contagious equine metritis bacterium. 708 71

Tendon tissue of eleven athletes suffering from insertion tendopathy and of two controls was examined. Part of the tissue was prepared for routine light microscopy, a part for enzyme histochemical staining of Nicotinamide-adenine-dinudeotide-diaphorase (NADP-diaphorase), lactate dehydrogenase (LDH), beta-glucuronidase and alkaline phosphatase. Small pieces of tissue were also prepared for electron microscopic examination. The removed tissue was edematous and mushy. The normally densely packed parallel or interwoven collagen bundles were loosened by edema, focal necrosis or hemorrhage. Infiltration of fatty tissue and granulation tissue was also present. The amount of acid mucopolysaccharides was markedly increased. The histochemical studies showed strong enzyme activity of NADP-diaphorase and LDH in normal tendon tissue as well as around areas of degeneration and in granulation tissue. beta-Glucuronidase and alkaline phosphatase was present, but in general with lesser activity than the above enzymes. The electron microscopic examination revealed marked degeneration of the fiber systems, focal necrosis, deposit of amorphous masses and mucopolysaccharides and focal mineralisation. The reparative zones showed proliferating capillaries, often with a collapsed lumen and prominent endothelial cells and basement membranes.
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PMID:Insertion tendopathy in athletes. A light microscopic, histochemical and electron microscopic examination. 712 23

The effect of the chronic intramuscular administration of some agents related to the S-adenosyl-L-methionine system on the hyperammonemia syndrome was evaluated. This experimental syndrome was induced in the rat by intraperitoneal administration of high doses of ammonium acetate (33, 100 and 300 mg/kg/day, 6 days a week for 80 days) followed by the assay of the activities of some cerebral enzymes involved in energy transduction. The enzymatic activities studied in the homogenate and in the mitochondrial fractions of brain tissue were: lactate dehydrogenase, citrate synthase, malate dehydrogenase, total NADH-cytochrome c reductase and cytochrome oxidase. All three doses of ammonium acetate induced significant modifications in the cerebral enzymatic activities. These doses reduced the activity of the total NADH-cytochrome c reductase both in the homogenate and in the mitochondrial fraction. On the other hand the activity of malate dehydrogenase was reduced limited to the two lower doses in the homogenate only. The simultaneous daily treatment (i.m.) with equimolar doses of substances involved in the S-adenosyl-L-methionine system (adenosine, methionine and S-adenosyl-L-methionine) did not cause any significant modification of the cerebral enzymatic activities associated with the administration of ammonium acetate at the three dose levels, thus confirming our previous results.
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PMID:Cerebral enzymatic activities during chronic hyperammonemia and treatment with S-adenosyl-L-methionine, adenosine and methionine in the rat. 725 Mar 59

The effect of a chronic (3 months) treatment with vincamine on the enzymatic activities related to energy transduction was studied on several areas of the cerebral cortex of dog brain. About enzymatic activities of the four different cortical areas, in controls, no difference was observed between the enzymatic activities evaluated in the crude mitochondrial fraction, with regard to both the tricarboxylic acid cycle (citrate synthase, malate dehydrogenase) and the electron transport chain (total NADH-cytochrome c reductase, cytochrome oxidase). On the contrary, in the homogenate, lactate dehydrogenase, malate dehydrogenase and acetylcholine esterase showed different maximal activities. In the crude mitochondrial fraction the intravenous treatment with the three different doses of vincamine failed to cause any significant change as compared to controls. On the contrary, with regard to the enzymatic activities evaluated in the homogenate in toto, the analysis of variance revealed an effect on cytochrome oxidase at the dose of 3 mg/kg intravenously.
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PMID:Effect of vincamine on some enzymatic activities from various areas of the beagle dog cerebral cortex. 729 73

1-Methoxy-5-methylphenazinium methyl sulfate (1-methoxyPMS) is a photochemically stable electron mediator between NAD(P)H and tetrazolium dyes. We have examined the efficiency of 1-methoxyPMS as an electron mediator in the assay of human lactate dehydrogenase (LDH, EC 1.1.1.27) and the activity staining of LDH isozymes after electrophoresis. The turnover number of 1-methoxyPMS as an electron mediator between NADH and nitrotetrazolium blue was 10--12 s-1, which is a value equal to that of PMS. Correlation coefficient between the estimated LDH activities of human sera obtained with 1-methoxyPMS and those obtained with diaphorase was 0.998. 1-MethoxyPMS successfully substituted for the unstable PMS in the activity staining of LDH isozymes of human serum, giving less background staining. We conclude that 1-methoxyPMS will be useful for routine methods of activity assay and activity staining of enzymes of diagnostic importance.
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PMID:Use of 1-methoxy-5-methylphenazinium methyl sulfate (1-methoxyPMS) in the assay of some enzymes of diagnostic importance. 735 52


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