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At least 1,693 records · Page 94Linked to original sources
PubMed1986

The reduction of dithiobis(2-nitrobenzoate) by rat liver mitochondria.

5,5'-Dithiobis(2-nitrobenzoate) (DTNB) is reduced in mitochondrial suspensions to 5-mercapto-2-nitrobenzoate (MNB) by 3-hydroxybutyrate and isocitrate. Although most of the MNB produced is found in the suspension medium, there is also some within the particles. The amount of MNB found in these fraction varies with the DTNB concentration used and is much lower if mitochondrial glutathione (GSH) is depleted with 1-chloro-2,4-dinitrobenzene. If hydroxybutyrate is present, the reduction of DTNB is increased by ATP and oligomycin. The pellet contains only a little MNB and GSH but these are considerably elevated by antimycin and rotenone as well as by ATP and oligomycin. If isocitrate is present, the reduction of DTNB is greatly stimulated by valinomycin, triethyltin and, to a lesser extent, oligomycin. MNB in the pellet falls and GSH concentrations are unchanged. The results suggest that with hydroxybutyrate (an NAD reducing substrate), the rate of reduction of DTNB is limited by the rate of regeneration of GSH while with isocitrate (an NADP reducing substrate) it is limited by the rate of export of MNB from the matrix.

3-Hydroxybutyric Acid↗
PubMed1992

Appearance of the Na(+)-motive terminal oxidase in Bacillus FTU grown under three different conditions lowering the delta mu H+ level.

The terminal oxidases and coupled Na+ transport have been studied in intact cells and inside-out subcellucar vesicles of alkalo- and halotolerant Bacillus FTU grown under different conditions. Cells grown at pH 7.5 are shown to possess a system of respiration-dependent Na+ transport which is (i) inhibited by protonophorous uncoupler and (ii) activated by the delta psi-discharging agent valinomycin, suggesting that the Na+ transport is due to cooperation of the H(+)-motive oxidase and Na+/H+ antiporter. On the other hand, growth under conditions lowering the delta mu H+ level, namely (i) pH 8.6, (ii) pH 7.5 in the presence of protonophore, and (iii) pH 7.5 in the presence of low cyanide concentrations results in appearance of terminal oxidase-supported Na+ transport which is stimulated by protonophores (the Na(+)-motive oxidase). In all three cases, the appearance of ascorbate (+ TMPD) oxidation resistant to low and sensitive to high cyanide concentrations was found to occur. It is concluded that not only alkaline pH but also other conditions which lower delta mu H+ can cause substitution of Na+ for H+ as a coupling ion.

Bacillus↗
PubMed1991

Central monoamine oxidase and phenolsulfotransferase activities in spontaneously hypertensive rats.

The activities of monoamine oxidase and phenolsulfotransferase in the hypothalamus and anterior pituitary gland of spontaneously hypertensive rats and the normotensive control (Wistar Kyoto rat) rats were investigated. The monoamine oxidase activity (determined using dopamine as substrate) in both these tissues was not significantly different between the normo- and hypertensive animals. Hypothalamic phenolsulfotransferase does not sulfate-conjugate dopamine at pH of 6.5 and pituitary phenolsulfotransferase does not sulfate-conjugate dopamine or 3,4-dihydroxyphenylacetic acid at the same pH. Hypothalamic phenolsulfotransferase activity determined using 3,4-dihydroxyphenylacetic acid as substrate was significantly higher in the spontaneously hypertensive than the Wistar Kyoto rats, while pituitary enzyme (determined using phenol as substrate) was the same in both strains of animals. We proposed that in the spontaneously hypertensive rats the higher level of hypothalamic phenolsulfotransferase could (by removing 3,4-dihydroxyphenylacetic acid as sulfated acid) increase the deamination of dopamine by monoamine oxidase. This could in turn result in the presence of high amount of sulfated 3,4-dihydroxyphenylacetic acid in the anterior pituitary gland reported in our earlier study, and be partly responsible for the reduced central dopaminergic activity found in the hypertensive rats.

Animals↗
PubMed1992

Quantitative bioassay using laser-monitored bacteria to assess toxicology and metabolism of bioactive Group IV compounds.

A new approach has been developed for assessing the toxicity and the metabolism of Group IV compounds and for other toxic substances that may interact with them at the molecular level. The approach is based upon the selective responses of sensitive biodetectors whose molecular interactions with a wide variety of toxic substances have been previously described and reported. Detection and quantitation of carbon, silicon, and tin-containing compounds has been accomplished using a laser-monitored bacterial bioassay. This system uses isogenic Bacillus subtilis strains that are genetically engineered to respond differentially to specific toxicants. The response of these biodetectors is monitored by differential light scattering of a laser that is integrated with a computerized system which collects and analyzes this data. The assay can routinely generate fully analyzed data for fixed time intervals, i.e. 60 or 90 min, or kinetic data so that the mechanisms of interactions can be elucidated.

Animals↗