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)

This communication presents the results obtained in tubular aggregates of 24 enzyme histochemical techniques for demonstrating activity of oxidoreductases, transferases, hydrolases and isomerases. The activity characteristics of the tubular aggregates in m. gluteus medius of 18 patients with diseases of the neuromuscular system were almost identical. A high activity of the mitochondrial enzymes, NADPH: tetrazolium oxidoreductase, NADH:tetrazolium oxidoreductase and cytochrome c oxidase, could be shown in the pathological structures, whereas the activity of the mitochondrial enzymes, glycerol-3-phosphate:menadione oxidoreductase, succinate:PMS oxidoreductase, malate:NAD+ oxidoreductase and isocitrate:NAD+ oxidoreductase, and the partial mitochondrial enzymes, malate:NADP+ oxidoreductase and isocitrate:NADP+ oxidoreductase, was very slight or even absent. There was a moderate to strong activity of the glycolytic enzymes lactate:NAD+ oxidoreductase, glyceraldehyde-3-phosphate:NAD+ oxidoreductase, phosphofructokinase, phosphoglucomutase and glucose phosphate isomerase. In contrast, the activity of alpha-glucan phosphorylase was slight. The activity of phosphogluconate:NADP+ oxidoreductase, glucose-6-phosphate:NADP+ oxidoreductase and 5'-nucleotidase was slight, whereas there was no activity of myosin ATPase and mitochondrial ATPase, acid phosphatase or alkaline phosphatase. The high activity of AMP-deaminase was very striking. The activity of peroxidase was moderate. Results obtained with adsorption studies point to adsorption of some of the enzymes studied to the tubular aggregates in vivo and this phenomenon very probably determined the histochemical characteristics of these structures.
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PMID:Histochemical features of tubular aggregates in diseased human skeletal muscle fibres. 317 98

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