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)

The effect of 28-day ethanol consumption on hamster liver microsomal electron transport systems and associated enzymatic activities has been examined. Microsomes isolated from ethanol-consuming hamsters showed increased levels of cytochrome P-450 and NADPH supported enzymatic activities. In contrast, reductions in the amount of cytochrome b5 and the NADH-supported rate of stearoyl-CoA desaturase were observed. NADH-cytochrome c reductase was decreased while a small increase in NADH-ferricyanide reductase was observed. These data suggest that decreased stearoyl-CoA desaturase activity is the result of lowered cytochrome b5 levels in microsomes isolated from ethanol-consuming hamsters.
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PMID:Differential effect of ethanol consumption on hamster liver microsomal electron transport systems. 286 Aug 17

Stearoyl-CoA desaturase activity in microsomes from lactating rat mammary gland is very low (0.05-0.15 nmol/min/mg of protein) regardless of lactating time. In such microsomes, reductase activities and content of cytochrome b5 are several-fold lower than in normal rat liver microsomes. Preincubation of the mammary microsomes with purified terminal desaturase gives a 55-fold stimulation of stearoyl-CoA desaturase activity, whereas preincubation with cytochrome b5 has no effect. However, preincubation of mammary microsomes with both cytochrome b5 and terminal desaturase results in a 200-fold stimulation of overall desaturation. These observations suggest that negligible stearoyl-CoA desaturase activity in lactating rat mammary microsomes is due to a cytochrome b5 content and the absence of terminal enzyme. The hepatic stearoyl-CoA desaturase activity increases 9-fold during lactation. There is little or no change in the NADH-cytochrome c reductase activity or in the concentrations of cytochrome b5 during this period, but the activity of the terminal desaturase increases with the increase of overall desaturation. These results suggest that liver is one of the more important sources of oleic acid for milk triglycerides.
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PMID:Stearoyl-coenzyme A desaturase activity in the mammary gland and liver of lactating rats. 612 66

Tetrahymena ISO cells, which have an unusually high level of iso odd-numbered fatty acids, were grown medium supplemented with various concentrations of isovalerate. There was a marked increase in the total proportion of iso odd-numbered fatty acids in supplemented whole cells (28.9 leads to 70.3%) and microsomes (37.7 leads to 84%), with a corresponding decrease in normal fatty acids, although no significant alteration of phospholipid composition was observed during 11 hr isovalerate-supplementation. Microsomal palmitoyl-CoA and stearoyl-CoA desaturase activities in isovalerate-supplemented cells decreased by 45.7% and 30.6% during 11 hr, respectively. NADH-cytochrome c reductase and NADH-ferricyanide reductase activities as well as the content of cytochrome b560ms, which is similar to mammalian microsomal cytochrome b5, were reduced in microsomes from 11 hr-supplemented cells, whereas NADPH-cytochrome c reductase activity was constant. It is suggested that the alteration of the cross-sectional area of lipid molecules in the bilayer, which results from the replacement of normal fatty acids with iso- 15:0 and iso- 17:1, would result in the decline of palmitoyl- and stearoyl-CoA desaturation in the isovalerate-supplemented cells, in order to maintain membrane fluidity at a functional level.
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PMID:Modification of microsomal lipid composition and electron transport enzyme activities in isovalerate-supplemented cells of novel Tetrahymena ISO. 641 Jan 44

Tetrahymena microsomes were solubilized with five different detergents and the effect on electron transport enzymes involved in fatty acid desaturation was studied. Cytochrome b560ms and NADPH-cytochrome c reductase were solubilized with a low concentration detergent (0.25%), in the order of sodium deoxycholate greater than Renex 690 greater than Triton X-100 greater than octylglucoside greater than sodium cholate, whereas all of these detergents at the high concentration (1%) could solubilize preferentially both enzymes (70-100%). Increasing the concentration of various detergents from 0.5 to 1.0% did not produce an incremental change in NADH-ferricyanide reductase solubilization. NADH-cytochrome c reductase system, which would be catalyzed by the cooperation action of NADH-ferricyanide and cytochrome b560ms, was relatively inactivated by all detergents. Compared to the other four detergents, octylglucoside has a much higher recovery of stearoyl-CoA desaturase activities in the supernatant. Our study suggests that octylglucoside may be more useful for the isolation in active form of cyanide-sensitive factor (CSF) from Tetrahymena microsomes.
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PMID:Studies on Tetrahymena microsomal electron transport systems: solubilization of microsomal electron transport enzymes involved in fatty acid desaturation. 643 62