PubMed Health⌕ Search

SEARCH · PubMed Health

Results for “Azides”

Explore indexed PubMed citations for clinical trials, systematic reviews and public health research. Read source abstracts and follow each citation to its original PubMed record.

Quote a phrase for an exact phrase match. Source license links do not imply unrestricted reuse.

At least 541 records · Page 30Linked to original sources
PubMed1963

Effect of azide and Ca ion on the reversible changes of protein configuration in stimulated nerves.

Working with sciatic nerves from the South American frog Calyptocephalella gayi we have been able to substantiate the finding of Ungar et al., that nerve proteins undergo a reversible denaturation concomitant with a train of nerve impulses. We also showed that 0.3 mM sodium azide is capable of impairing the reversibility of those changes. Furthermore, 10 meq/liter of calcium ion applied to extracts of resting nerves induce configurational rearrangements in the proteins similar to those produced during stimulation. We also proved that nerves previously kept in low calcium Ringer's solution do not show configurational changes upon stimulation. A tentative interpretation of the results described is that the configurational changes are a consequence of the extra influx of calcium ion due to nerve impulse propagation.

Action Potentials↗
PubMed1999

An azide-insensitive superoxide dismutase from a hyperthermophilic archaeon, Sulfolobus solfataricus.

The superoxide dismutase (SOD) gene of Sulfolobus solfataricus, a hyperthermophilic archaeon, was cloned and expressed in Escherichia coli, and its gene product was characterized. When the protein was expressed in E. coli, it formed a homodimer that contained both Mn and Fe. Metal reconstitution experiments of the SOD with Fe or Mn showed that only the Fe-reconstituted SOD was active. Substitution of Tyr88 to Phe did not affect the metal specificity of the enzyme. The Fe-reconstituted SOD was extremely resistant to thermal denaturation; e.g. 96% of the initial activity was retained after heating at 95 degreesC for 2 h. Fe-reconstituted SOD was not inhibited by azide, but fluoride inhibition was observed. This suggests that some steric hindrance in the substrate funnel of the enzyme prevents the access of N3- but allows O2- and F- access to the active site.

Amino Acid Sequence↗
PubMed1984

An anti-I cold auto-agglutinin enhanced in the presence of sodium azide.

Difficulty in determining the ABO blood group led to the discovery of an anti-I cold auto-agglutinin in the serum of a blood donor. The peculiarity of this antibody is that its activity is enhanced in the presence of a preservative found in manufactured anti-sera: sodium azide. At 4 degrees C, the auto-antibody agglutinates RBCs even without NaN3 but the drug increases its effect in the cold. At 22 degrees C, the drug is necessary for the adsorption of the antibody on red cells.

Adult↗
PubMed1983

Elimination of artifactual acetaldehyde in the measurement of human blood acetaldehyde by the use of polyethylene glycol and sodium azide: normal blood acetaldehyde levels in the dog and human after ethanol.

A new procedure is described for the preparation of human blood samples for analysis of acetaldehyde and ethanol by head space gas chromatography. High concentrations of polyethylene glycol were used to remove the hemoglobin and approximately 50% of the plasma protein. Artifactual formation of acetaldehyde from ethanol was inhibited by sodium azide. Using this method, no artifactual acetaldehyde was detectable in human, dog, sheep, and rat blood when spiked with ethanol in final concentrations of 65 mM. The recovery of added acetaldehyde was approximately 80% for human dog, and sheep blood, whereas it was only 30% for rat blood. Following ethanol administration, acetaldehyde levels were determined in blood taken from the pulmonary artery and descending aorta of the dog and human, and also from the hepatic vein of the latter. The relative blood acetaldehyde concentrations at these sites were hepatic vein greater than pulmonary artery greater than descending aorta.

Acetaldehyde↗
PubMed1984

Relation between the iodine azide test and the TTCA test for exposure to carbon disulphide.

Exposure to carbon disulphide (CS2) in a viscose plant was measured by personal monitoring and by application of the iodine azide test and quantification of 2-thio-thiazolidine-4-carboxylic-acid (TTCA) in urine samples. A relation was found between the rise in urinary TTCA concentration during the workshift and the exposure index E1. The correlation (r) between the exposure index and the atmospheric concentrations of CS2 in workroom air below 100 mg CS2/m3 was 0.59 (n = 9). The correlation between the increase in TTCA concentrations during the workshift and the atmospheric CS2 concentrations was found to be higher when urine samples at the end of the workshift with creatinine concentrations below 1 mg/ml and above 3 mg/ml were disregarded (from r = 0.61; n = 20 to r = 0.84; n = 14). A high correlation was found (r = 0.86; n = 13) when the end of workshift urine samples were analysed, provided that their creatinine concentrations are not beyond the limits given above.

Azides↗
PubMed1993

Sodium azide protects against ischemia-induced acute renal failure in rats.

Sodium azide (AZ) is a nitrovasodilator with diverse biochemical properties. We found that low doses of AZ led to a profound protective effect against postischemic, acute renal failure (ARF) in rats. AZ, given at 250 micrograms/kg iv, before 25 min of renal artery occlusion (RAO) and again before reperfusion, conferred almost complete protection against loss of kidney function determined 18 h after RAO. The effect of AZ was evidenced by a higher creatinine clearance (+348%) and lower levels of blood urea nitrogen (-69%) and histological renal damage (-50%) compared with ischemic control animals. Indexes of kidney function in AZ-treated animals subjected to RAO were not significantly different from those of nonischemic control animals. Two other nitrovasodilators, sodium nitroprusside and hydralazine, at doses which produced decreases in blood pressure similar to that of AZ, were ineffective at preventing ARF. The beneficial effect of AZ may be due to its known ability to inhibit one or more enzymes including adenosinetriphosphatase, cytochrome-c oxidase, and myeloperoxidase.

Acute Kidney Injury↗
PubMed1989

Atrial natriuretic peptide and sodium azide dependent guanylate cyclase activities in placentas from normal and severely toxemic patients.

Particulate guanylate cyclase is stimulated by several hormones through receptor-dependent and by nitrosovasodilators through receptor-independent mechanisms. A subtype of atrial natriuretic peptide (ANP) receptors is coupled to guanylate cyclase. It has been shown that there is a down-regulation of the affinity of ANP receptors to alpha-hANP in placental plasma membranes obtained from severely toxemic patients. We have asked the question whether these changes are associated with a down-regulation of ANP-dependent guanylate cyclase activity. Guanylate cyclase was determined by in vitro experiments using a placental plasma membrane fraction obtained from normal and from severely toxemic patients. The presence of ANP-dependent placental guanylate cyclase activity was demonstrated both in normal and toxemic placentas. Although basal guanylate cyclase activity was not influenced by toxemia of pregnancy, there was a significant decrease in the maximum stimulation of this enzyme by alpha-hANP (104.81 +/- 12.02% (n = 4) vs 49.41 +/- 8.73% (n = 7) for normal and toxemics, respectively). Finally, stimulation by a nitrosovasodilator, sodium azide (NaN3), was also lower in toxemic placentas than in normal controls. These observations extend our previously reported results on placental ANP receptor function but also suggest the presence of a possibly receptor-independent decrease in guanylate cyclase activity in toxemic placentas.

Adult↗
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↗
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↗
PubMed1990

Kinetics and thermodynamics of oxygen, CO, and azide binding by the subcomponents of soybean leghemoglobin.

Leghemoglobin shows extreme high affinity behavior in the binding of both oxygen and CO. We have determined the temperature dependence of the rate constants for ligation of oxygen and CO and from these data the thermodynamics (delta G0, delta H0, delta S0) of ligation for the purified components of soybean leghemoglobin. X-ray crystallography has shown that the heme cavity can easily accommodate ligands the size of nicotinate, and analysis of extended x-ray absorption fine structure data has shown that the Fe atom is in the mean plane of the heme in the leghemoglobin-CO complex. Ligation of oxygen and CO are in accord with this picture in that the Ea for oxygen binding is that expected for a diffusion controlled reaction and delta S0 for the ligation of both CO and oxygen is consistent with the simple immobilization of the ligand at the Fe, with no evidence for significant conformational changes in the protein or changes in solvation. At 20 degrees C the rate constants for oxygen and CO binding vary by 26-44% among the eight leghemoglobin components. For azide binding the variation is a factor of 2. These variations appear to arise from amino acid substitutions outside either the heme cavity or the two major paths for ligand entry to the heme. The distribution of leghemoglobin components varies with the age of the soybean nodule during the growing season. The changes in composition alone, however, would only allow the concentration of free oxygen to vary by about 3%. This finding calls into question models that ascribe a significant functional role to changes in the distribution of leghemoglobin components in regulating oxygen concentration in the nodule.

Azides↗
PubMed1989

Effect of Emblica officinalis Gaertn. (Indian gooseberry) fruit extract on sodium azide and 4-nitro-o-phenylenediamine induced mutagenesis in Salmonella typhimurium.

Water, acetone and chloroform extracts of E. officinalis fruit reduced sodium azide and NPD induced his+ revertants significantly in TA100 and TA97 a strains respectively of S. typhimurium. The chloroform extract was less active as compared to water and acetone extracts. Autoclaving of water extract for 15 min did not reduce its activity. The enhanced inhibitory activity of the extracts on pre-incubation suggests the possibility of desmutagens in the extracts. Besides ascorbic acid, a constituent of the extract, the role of other antimutagenic factors in the extract cannot be ruled out.

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↗
PubMed1983

Sodium azide enhancement of interleukin-2 production.

The production of large quantities of Interleukin-2 (IL-2) from normal human lymphocytes has been limited by the short production and release period, as well as its absorption by the responsive cell population. We report the utilization of sodium azide (NaN3, 0.01% final concentration) to allow continued production of IL-2 as long as 72-96 hr and thereby increase the yield significantly. Cell cycle analysis performed by flow cytometry indicates that NaN3 blocks cells at the G0-G1 transition and the G1-S transition, depending on the time of addition of NaN3 to the cultures.

Animals↗
PubMed1993

[Antimutagenic action of superoxide dismutase on sodium azide- and nitrosoguanidine-induced mutagenesis in Salmonella typhimurium TA 1535].

It was shown that superoxide dismutase (SOD) decreased the mutagenic action of sodium azide (NaN3) and N-methyl-N'-nitro-N-nitrosoguanidine in Salmonella typhimurium TA1535. Catalase and quenchers of hydroxyl radicals showed, unlike SOD no effect on the mutagenicity of NaN3. Cell extract from propionic acid bacteria also possessed the antimutagenic activity, only partially depending on the SOD activity.

Antimutagenic Agents↗
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↗
PubMed2003

Biocompatibility of collagen membranes crosslinked with glutaraldehyde or diphenylphosphoryl azide: an in vitro study.

Crosslinking of collagen biomaterials increases their resistance to degradation in vivo. Glutaraldehyde (GA) is normally used to crosslink collagen biomaterial, but is often cytotoxic. Diphenylphosphoryl azide (DPPA) has recently been proposed as reagent, but little is known about its effects on cell behavior. In this study, we determined which collagen membrane was the most biocompatible: Paroguide which is crosslinked with DPPA and contains chondroitin sulfate; Opocrin which is crosslinked with DPPA; Biomed Extend which is crosslinked with GA; and Bio-Gide which is left untreated. Cell proliferation and extracellular matrix macromolecule deposition were evaluated in human fibroblasts cultured on the membranes. The GA-crosslinked Biomed Extend membrane and the not-crosslinked Bio-Gide membrane reduced cell growth and collagen secretion compared with DPPA-crosslinked biomembranes. When Paroguide and Opocrin were compared, better results were obtained with Paroguide. The greatest amount of transforming growth factor beta1, a growth factor involved in extracellular matrix macromolecule accumulation and in tissue regeneration, was produced by cells cultured on Paroguide, with Opocrin second. Our data suggest that the DPPA method is more biocompatible than the GA for crosslinking collagen biomaterials and that membranes made of collagen plus chondroitin sulfate are better than membranes made of pure collagen.

Azides↗
PubMed1979

Pyrenesulfonyl azide as a fluorescent label for the study of protein-lipid boundaries of acetylcholine receptors in membranes.

Acetylcholine receptor (AcChR) enriched membrane fragments from Torpedo californica electroplax were labeled by in situ photogenerated nitrenes from a hydrophobic fluorescent probe, pyrene-1-sulfonyl azide. Preferential photolabeling of membrane proteins, mainly AcChR, has been achieved and there is a pronounced exposure of the 48,000 and 55,000 molecular weight subunits of AcChR to the lipid environment of the membrane core. Covalent attachment of the photogenerated fluorescence probe does not perturb the alpha-neurotoxins' binding properties of membrane-bound AcChR or the desensitization kinetics induced by prolonged exposures to cholinergic agonists. Non-covalent photoproducts can be conveniently removed from labeled membrane preparations by exchange into lipid vesicles prepared from electroplax membrane lipids. Fluorescence features of model pyrene sulfonyl amide derivatives, such as fine vibrational structure of emission spectra of fluorescence lifetimes, are highly sensitive to the solvent milieu. The covalently bound probe shows similar fluorescence properties in situ. PySA photoproducts have great potential to spectroscopically monitor neurotransmitter induced events on selected AcChR subunits exposed to the hydrophobic environment of membranes.

Acetylcholine↗