Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:1.6.5.2 (NQO1)
 6,196 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The method of purification up to homogenous states and properties of NADP-reductase of purple bacteria Thiocapsa roseopersicina, strain BBS, are described. The molecular weight of NADP-reductase is about 47 000; it is flavoprotein consisting of two subunits. Atebrim and chloromercury bensoate inhibit the activity of NADP-reductase (34% and 33--60%, respectively). The enzyme is specific to NADPH; it catalyzes menadion-reductase reaction, diaphorase reaction of benzyl viologen reduction, oxidation of reduced benzyl viologen in the presence of NADP, reduction of ferredoxin and cytochrome c in the presence of NADPH, but it is not capable to catalyze transhydrogenase reaction.
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PMID:[Purification and properties of NADP-reductase of phototropic bacteria Thiocapsa roseopersicina]. 2 Jan 66

Unlike Rhodospirillum rubrum, the highly purified preparations of NADP-reductase Thiocapsa roseopersicina are capable of reduction of cytochrome c though they do not catalyse diaphorase reaction in the presence of methyl viologen or benzyl viologen and NADH. T. roseopersicina reductase has more high temperature optimum (50-65 degrees) and more high thermal stability (65 degrees) and it is capable to catalyse diaphorase and menadione-reductase reactions under more high pH values (11.0-12.0) than NADP-reductase of R. rubrum. NADP-reductase of T. roseopersicina is more stable under storing than the enzyme from R. rubrum: the semi-inactivation period of the enzyme when storing in Ar or the air is about 10 and 4 days, respectively, and it takes about three days for R. rubrum.
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PMID:[Comparative study of NADP-reductase properties in two species of purple bacteria]. 2 Sep 91

Immunization of rabbits with botulinus anatoxin containing a number of proteins of bacterial origin causes a statistically significant increase in the activity of succinate dehydrogenase, NAD diaphorase and NADP diaphorase as early as after 24 hours. After 5-7 days, the activity of all mitochondrial enzymes drops below the control level and returns to normal by the 14th day. The activity of glucose 6-phosphatase decreases significantly already 24 hours after immunization and returns to normal by the end of the 7th day. The mechanism of excretion of foreign protein in the kidneys of immunized animals is discussed.
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PMID:Histochemical investigation of some mitochondrial and microsomal enzymes in the kidneys of rabbits immunized with type B botulinus anatoxin. 3 81

Ovarian cycle in albino rats was applied to ascertain the problem of the relationship between the salivary and endocrine glands, and also of the extent of participation of individual components of the salivary glands with different functional orientation in the endocrine regulation of individual components of the salivary glands. The content of protein, mucopolysaccharides, DNA, and RNA, the activity of NAD- and NADP-diaphorase, alkaline phosphatase, malate and isocitrate dehydrogenase, alpha-leucine-aminopeptidase was studied. Cytospectrophotometric analysis showed that synchronous changes in the activity of the enzymes under study occurred in all the portions of the salivary glands, depending on the ovarian cycle phases. Of the four successive phases of the cycle the greatest activity of the enzymes and of the protein and mucopolysaccharide content was noted during the proestrus and metaestrus. Different metabolic processes were observed in the salivary ducts in comparison with other parts of the gland; this was apparently connected with peculiarities of the secretion and hormone production.
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PMID:[Quantitative histoenzymologic characteristics of the submaxillary salivary glands of white rats during an ovarian cycle]. 14 76

The method of visual quantitative estimation was employed to determine the index of enzymes activity in embryonal cells cultures infected with Rous virus. In early terms (1-7 days after infection) a moderate production of diformazane was noted in the presence of glucoso-6-phosphatiosomerase, phosphoglucomutase, pyruvatoxidase, NAD. H2- and NADP. H-2-diaphorase, other enzymes showing no distinquishable deviations in the activity, as compared with the normal culture. In later terms (13-27 days) during the proliferation of the transformed cells there was found an increased level of the glycolysis enzymes activity, pentose cycle, hydrolysis of ortho-phosphoric acid monoethers and reduced lemon acid cycle and tissue respiration. Cytoplasmatic vacuoles formed in the transformed cells seem to represent hypertrophic lysosomes and phagolysosomes.
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PMID:[Quantitative cytochemical detection of enzymes in cultured cells following infection with Rous virus]. 17 56

Asparagusate dehydrogenases I and II and lipoyl dehydrogenase have been obtained in homogeneous state from asparagus mitochondria. They are flavin enzymes with 1 mol of FAD/mol of protein. Asparagusate dehydrogenases I and II and lipoyl dehydrogenase have s20,w of 6.22 S, 6.39 S, and 5.91 S, respectively, and molecular weights of 111,000, 110,000, and 95,000 (sedimentation equilibrium) or 112,000, 112,000, and 92,000 (gel filtration). They are slightly acidic proteins with isoelectric points of 6.75, 5.75, and 6.80. Both asparagusate dehydrogenases catalyzed the reaction Asg(SH)2 + NAD+ equilibrium AsgS2 + NADH + H+ and exhibit lipoyl dehydrogenase and diaphorase activities. Lipoyl dehydrogenase is specific for lipoate and has no asparagusate dehydrogenase activity. NADP cannot replace NAD in any case. Optimum pH for substrate reduction of the three enzymes are near 5.9. Asparagusate dehydrogenases I and II have Km values of 21.5 mM and 20.0 mM for asparagusate and 3.0 mM and 3.3 mM for lipoate, respectively. Lipoyl dehydrogenase activity of asparagusate dehydrogenases is enhanced by NAD and surfactants such as lecithin and Tween 80, but asparagusate dehydrogenase activity is not enhanced. Asparagusate dehydrogenases are strongly inhibited by mercuric ion, p-chloromercuribenzoic acid, and N-ethylmaleimide. Amino acid composition of the three enzymes is presented and discussed.
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PMID:Asparagusate dehydrogenases and lipoyl dehydrogenase from asparagus mitochondria. Physical, chemical, and enzymatic properties. 18 3

Quantitative activity of oxidative-reductive and hydrolytic enzymes obtained during operation was investigated in different parts of the human submandibular salivary glands. Quantitative estimation of enzymic activity was done by photometry of the negatives prepared on MY-phi-6. Comparative examination of enzymatic activity made it possible to state that according to the peculiarities of metabolic processes, the cells of striated and intralobular secreting ducts are similar to the cells of the secreting terminal parts. A high activity of NADP-diaphorase, G-6-PhDG and acid phosphatase in the epithelium of the secreting ducts, and parallelism, stated between histoenzymatic and morphologic criteria of functional activity proved the participation of these structural-functional units in secret-producing processes. A high activity of NAK-diaphorase, LDG and acid phosphatase in all the parts and in the secreting ducts system, in particular, ensures, besides the processes of protein secret formation, an active transport of natrium and potassium, formation of final saliva and its discharge.
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PMID:[Quantitative histoenzymologic characteristics of the human submandibular salivary glands]. 19 5

Experiments were conducted on rabbits. A study was made of the activity of the redox enzymes--glucose-6-phosphate dehydrogenase (G-6-PDH), lactate dehydrogenase (LDH), succinate dehydrogenase (SDH), malate dehydrogenase (MDH), NAD-and NADP-diaphorases, cytochromeoxidase (CCO), alpha-glycerophosphate dehydrogenase (alpha-GPDH) in the supraoptic and paraventricular nuclei of the hypothalamus and the posterior lobe of the hypophysis under conditions of stimulation and removal of the superior cervical sympathetic ganglia. There was revealed a correlation between the activity of the tissue respiration enzymes (SDH, MDH, NAD- and NADP-diaphorase, CCO) and the functional condition of the hypothalamo-neurohypophysial neurosecretory system. However, the enzymes of the pentose-phosphate (G-6-PDH) and glycerophosphate shunt (alpha-GPDH) and also of the anaerobic way of oxidation (LDH) reacted nonspecifically on the induced effects.
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PMID:[Effect of removal and stimulation of the superior cervical sympathetic ganglia on the activity of oxidation-reduction enzymes in the neurosecretory cells of the anterior hypothalamus in rabbits]. 20 40

The authors have studied the enzymhistochemical and ultrastructural pictures of tenocytes of adult human tendons. High succinate dehydrogenase, cytochrome oxidase, TPN-diaphorase, lactate dehydrogenase and glucose-6-phosphate dehydrogenase activity were found, as indicated both oxidativ, anaerobic and pentose-phosphate shung activity. Phosphorylase and glutamate dehydrogenase activity was medial, lipase and alcaline phosphatase activity was slight. In tenocytes well developed rough endoplasmic reticulum and GOLGI apparatus, large amount of free ribosomes were found.
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PMID:Histochemical and ultrastructural study of adult human tendon. 23 84

The activity of some enzymes in T- and B-lymphocytes from the spleen of CBA mice was investigated. T-cell suspension was obtained by using a modified Kedar et al. method based on immunosorption. EAC-rosette forming cells were studied in the capacity of B-cells. The activity of all the enzymes examined proved to be higher in T-lymphocytes than in B lymphocytes; the greatest difference was noted in the activity of NADP.H2-diaphorase, and the least--in the activity of NAD.H2-diaphorase.
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PMID:[Activity of a number of enzymes in the splenic T- and B-lymphocytes of CBA strain mice]. 31 70


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