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PubMed1992

[Efficiency of inhibitors (phenylethanol, nalidixic acid, sodium azide)in the isolation of strictly anaerobic bacteria from a polymicrobial specimen].

The efficacy of inhibitors (PEA, Ac Nal, Az de Na) in the isolation of strict anaerobes in polymicrobial sample. The efficacy of three inhibitors to select strict anaerobic bacteria in the polymicrobial sample had been studied. First step: The most frequent anaerobes encountered in the infections are isolated in the agar Columbia containing the different inhibitors. This step allowed us to check the inhibition of the germ we have to isolate. Next step: polymicrobial mixtures were made. The composition of which is very similar to the samples we receive in the laboratory. The swarming Proteus is the facultative anaerobic germ which gives us difficulties when isolating strict anaerobic bacteria. Then, the different mixtures were isolated separately in the agar in which the inhibitors were added. The plates containing Azide of Na and PEA gave us the best results.

Azides↗
PubMedDate not supplied

[Inhibition of the antioxidative activity of plasma by sodium azide].

Powerful antioxidant activity of human plasma was demonstrated by measuring the thiobarbituric acid reaction and Fe+2-induced chemiluminescence. Inhibition of lipid peroxidation was shown both for plasma lipids and for the suspension of egg lipoproteins, which was taken as a model system. The inhibitory effect of plasma peroxidation was removed by azide Na taken in the concentration of 0.5 mg/ml, but caeroplasmin activity in the plasma was completely suppressed at NaN3 concentration equal to 0.1 mg/ml. A low correlation (r = 0.75) between caeruloplasmin activity in the blood plasma and extent of chemiluminescence activation obtained in the presence of NaN3 was found. The presented data led to an assumption that only a part of lipid peroxidation inhibitors in the plasma can be attributed with caeruloplasmin.

Apolipoproteins B↗
PubMed1992

[A stereoscopic analysis of centrosome structure in the cells of a tissue culture under the action of energy metabolism inhibitors. I. 2,4-Dinitrophenol, deoxyglucose, sodium azide and the calcium ionophore A23187].

A 30-min action of energy transfer inhibitors (2,4-dinitrophenol, deoxyglucose, azide and calcium ionophore A23187) on tissue culture cells results in a significant increase in the quantity of microtubules around the centrosome. After the action of all the inhibitors, mostly increases the number of long microtubules with free proximal end oriented towards the centrosome. It is suggested that energy transfer inhibitors may stimulate foundation of microtubules on the centrosome and stabilize free microtubules, while they exert no effect on the frequency of detachment of microtubules from the centrosome.

2,4-Dinitrophenol↗
PubMed1996

[Two components of sodium-azide insensitive Mg2+,ATP-dependent Ca2+ transport in ureteral smooth muscle membrane structures].

The effects of Ca(2+)-precipitating anions (oxalate and phosphate) and effective inhibitors of endo/sarcoplasmic reticulum calcium pump (thapsigargin and cyclopiazonic acid) on azide-insensitive (5 mM) Mg2+,ATP-dependent Ca2+ accumulation in microsomes of ureter smooth muscle cells were studied. Oxalate (0-20 mM) and phosphate (0-60 mM) stimulate Mg2+,ATP-dependent Ca2+ accumulation. Thapsigargin and cyclopiazonic acid at 100 nM and 20 microM, respectively, completely inhibited (i.e., down to the level in the absence of oxalate) Ca2+ accumulation activated by 10 nM oxalate. These inhibitors only partially inhibited Ca2+ accumulation activated by 40 mM phosphate. Mg2+,ATP-dependent Ca2+ accumulation in microsomes, which is inhibited by thapsigargin and cyclopiazonic acid and activated by oxalate or phosphate, can result from functioning of calcium pump in endoplasmic reticulum of ureter myocytes. The inhibition constant, Ki, was calculated by the method of Hill and it was 0.3 nM and 0.2 microM for thapsigargin or cyclopiazonic acid, respectively. Mg2+,ATP-dependent Ca2+ accumulation in microsomes, which is insensitive to thapsigargin or cyclopiazonic acid and activated by phosphate, can result from functioning of calcium pump in plasma membranes of ureter myocytes.

Adenosine Triphosphate↗
PubMed2004

[Sodium azide].

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Biomarkers↗