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)

Activity of succinate dehydrogenase, alpha-glycerophosphate dehydrogenase, NAD2- and NADP2-diaphorases and acid phosphatase in lymphocytes of the peripheral blood as well as malonic dialdehyde and alpha-tocopherol, as parameters of lipid peroxidation defense, were studied in 49 patients with different forms of pulmonary tuberculosis and in 17 practically and clinically healthy subjects. Patients with focal pulmonary tuberculosis presented drop of succinate dehydrogenase and NAD2-diaphorase activity and rise of alpha-glycerophosphate dehydrogenase and NADP2-diaphorase activity in lymphocytes. Parameters of malonic dialdehyde and alpha-tocopherol in patients and healthy subjects had no difference. Patients with infiltrative and fibrocavernous pulmonary tuberculosis had drastic suppression of energy enzymes and sharp rise of acid phosphatase activity in lymphocytes, which correlated with a significant rise of malonic dialdehyde level and decrease of blood serum alpha-tocopherol. There was a tendency to an increase in energy enzymes activity and decrease of acid phosphatase activity 3-4 months after chemotherapy, which was followed by the clinical improvement of patients' condition. Direct dependence was found between the normalization of enzyme activity of lymphocytes and diminution of lipid peroxidation processes.
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PMID:[Lymphocyte enzymes, activity of lipid peroxidation processes and the antioxidant protection of patients with tuberculosis of the lungs]. 146 3

Two types of the NADH-quinone reductase were isolated from Thermus thermophilus HB-8 membranes, by use of the nonionic detergent, dodecyl beta-maltoside, and NAD-agarose affinity, DEAE-cellulose, hydroxyapatite, and Superose 6 column chromatography. One of these (NADH dehydrogenase 1) is a complex composed of 10 unlike polypeptides, and the other (NADH dehydrogenase 2) exhibits a single band (Mr 53,000) upon sodium dodecyl sulfate-polyacrylamide gel electrophoresis. The NADH-ubiquinone-1 reductase activity of the isolated NADH dehydrogenase 1 was about 14 times higher than that of the dodecyl beta-maltoside extract and partially rotenone sensitive. The NADH-ubiquinone-1 reductase activity of the isolated NADH dehydrogenase 2 was about 30-fold as high as that of the dodecyl beta-maltoside extract and rotenone insensitive. The purified NADH dehydrogenase 1 contained noncovalently bound FMN, non-heme iron, and acid-labile sulfide. The ratio of FMN to non-heme iron to acid-labile sulfide was 1:11-12:7-9. The high content of iron and labile sulfide is suggestive of the presence of several iron-sulfur clusters. The purified NADH dehydrogenase 2 contained noncovalently bound FAD and no non-heme iron or acid-labile sulfide. The activities of both NADH dehydrogenases were stable at temperatures of greater than or equal to 80 degrees C. The occurrence of two distinct types of NADH dehydrogenase as a common feature in the membranes of various aerobic bacteria is discussed.
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PMID:Purification and characterization of two types of NADH-quinone reductase from Thermus thermophilus HB-8. 337 42