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PubMed1981

Infecundity and dominant lethal mutations induced in Musca domestica L. by sodium azide (NaN3).

Results of our study suggest that sodium azide is effective in the induction of sterility and dominant lethal mutations in both sexes of M. domestica L. When treated males were crossed with nontreated females, 100% dominant lethal mutations and 72.3% infecundity were found, whereas in the crosses of nontreated males and treated females, 82.5% dominant lethal mutations and 33.1% infecundity were found. This showed that males are more sensitive to sodium azide than females.

Animals↗
PubMed1997

The Ames miniscreen assay: volatility of sodium azide can cause an increase in the reversion frequencies of adjacent, untreated wells.

Sodium azide, when added to wells adjacent to untreated wells, caused an increase in the reversion rate of Salmonella typhimurium TA100 in a 12-well plate format. Increases in the reversion frequency in adjacent, untreated wells were observed when a single well on the plate was treated with as little as 1 microg of sodium azide. This effect is probably caused by the hydrolysis of sodium azide to form hydrazoic acid. Hydrazoic acid has a boiling point of 37 degrees C and, thus, would become a diffusible gas during the incubation of the plates. Our findings suggest that a diffusible gas is present and that this gas has the ability to contaminate nearby wells when using the multiwell version of the Ames assay. Furthermore, it may be prudent to isolate all positive controls and negative controls on separate plates with no test material since a volatile test material could produce spurious results in the Ames miniscreen.

Azides↗
PubMed1990

Inactivation of lignin peroxidase by phenylhydrazine and sodium azide.

Lignin peroxidase (LiP) is rapidly inactivated in a concentration-dependent manner by H2O2 and either phenylhydrazine or sodium azide. Full inactivation of isozyme 2b (H8) requires approximately 50 eq of phenylhydrazine or 80 eq of sodium azide. Anaerobic incubation of isozyme 2b with [14C]phenylhydrazine and H2O2 results in 77% loss of catalytic activity and covalent binding of 0.45 mol radiolabel/mol of enzyme. Comparable but not identical results are obtained with an isozyme mixture. A lag period is observed before the peroxidative activity can be measured when an aliquot of an incubation with sodium azide is diluted into the mixture used to assay residual catalytic activity. This lag is associated with reversible accumulation of a catalytically inert species with a Compound III-like spectrum. No meso-phenyl, iron-phenyl, or N-phenyl adducts are formed with phenylhydrazine but a low yield of what appears to be delta-meso-azidoheme is obtained with sodium azide. LiP is thus less susceptible to meso heme additions and more susceptible to oxidative heme degradation than horseradish peroxidase. The data suggest that the active of LiP resembles the closed structure of horseradish peroxidase more than it does the open structure of the globins, catalase, chloroperoxidase, or cytochrome P450.

Azides↗
PubMed1995

Role of sodium azide in reducing nonspecific color development in enzyme immunoassays.

Improved enzyme immunoassay (EIA) procedures achieved by incorporating sodium azide during predilution of serum samples in a solid-phase EIA for the detection of anti-Toxoplasma antibody in swine using a peroxidase conjugate and in all washes of a bovine brucellosis rapid card test EIA using alkaline phosphatase conjugate are reported. Without this modification, substantial background interference was encountered that showed direct correlation with the degree of hemolysis of the serum samples. Anti-Toxoplasma gondii antibody-negative samples, separated by subjective groupings based on degree of hemolysis, into "clear", "slight", and "gross/total" samples, had a mean +/- standard deviation of 0.150 +/- 0.072, 0.187 +/- 0.105, and 0.232 +/- 0.108, respectively. The incorporation of sodium azide during the initial step of serum dilution dramatically eliminated the background, giving a mean +/- standard deviation of 0.079 +/- 0.029, 0.076 +/- 0.022, and 0.081 +/- 0.029, respectively. The level of endogenous peroxidase activity, a possible factor for this nonspecific interference, was considerably elevated in some of the swine sera. The clear, slight, and gross/total categories had relative levels of 1%, 2%, and 51% peroxidase activity compared to the conjugate peroxidase activity of 100%. Whereas sodium azide could be used only in sample predilution in the swine toxoplasmosis peroxidase-conjugate test, in the bovine brucellosis alkaline phosphatase-conjugate card test it could be used in all wash cycles. Many brucellosis card test results were visually uninterpretable because of significant background color when the manufacturer's wash reagent was used. The substitution of a wash reagent containing sodium azide eliminated background color, giving a visually unambiguous test.

Animals↗
PubMed1977

Interference of sodium azide with measurement of serum uric acid by the direct acid ferric reduction procedure.

We examined the effect of sodium azide on the quantitation of serum uric acid by the direct acid ferric reduction procedure. Ferric phenanthroline was used as redox indicator. Sodium azide, in a concentration commonly used as preservative (2 g/liter, 27.2 mmol/liter), increased the absorption at 505 nm and increased apparent uric acid values in specimens, as shown by calculations based on an azide-free standard. Spectral studies indicated that this interference was a result of the color produced by sodium azide in the reaction mixture. The mechanism for azide interference was the interaction of sodium azide and ferric ions to form ferric azide, which also absorbs extensively at 505 nm.

Azides↗
PubMed1995

The inhibitory effect of 3-amino-1,2,4-triazole on relaxation induced by hydroxylamine and sodium azide but not hydrogen peroxide or glyceryl trinitrate in rat aorta.

1. In this study we investigated the role of catalase in relaxation induced by hydroxylamine, sodium azide, glyceryl trinitrate and hydrogen peroxide in isolated rings of rat aorta. 2. Hydrogen peroxide (1 microM-1 mM)-induced concentration-dependent relaxation of phenylephrine (PE)-induced tone in endothelium-containing rings. In endothelium-denuded rings, however, higher concentrations (30 microM-1 mM) of hydrogen peroxide were required to produce relaxation. The endothelium-dependent component of hydrogen peroxide-induced relaxation was abolished following pretreatment with N(O)-nitro-L-arginine methyl ester (L-NAME, 30 microM). L-NAME (30 microM) had no effect, however, on hydrogen peroxide-induced relaxation in endothelium-denuded rings. 3. Pretreatment of endothelium-denuded rings with catalase (1000 u ml-1) blocked relaxation induced by hydrogen peroxide (10 microM-1 mM). The ability of catalase to inhibit hydrogen peroxide-induced relaxation was partially blocked following incubation with 3-amino-1,2, 4-triazole (AT, 50 mM) for 30 min and completely blocked at 90 min. 4. Pretreatment of endothelium-denuded rings with methylene blue (MeB, 30 microM) inhibited relaxation induced by hydrogen peroxide (10 microM-1 mM), sodium azide (1-300 nM), hydroxylamine (1-300 nM) and glyceryl trinitrate (1-100 nM) suggesting that each acted by stimulation of soluble guanylate cyclase. 5. Pretreatment of endothelium-denuded rings with AT (1-50 mM, 90 min) to inhibit endogenous catalase blocked relaxation induced by sodium azide (1-300 nM) and hydroxylamine (1-300 nM) but had no effect on relaxation induced by hydrogen peroxide (10 microM-1 mM) or glyceryl trinitrate (1-100 nM). 6. In a cell-free system, incubation of sodium azide (10 microM-3 mM) and hydroxylamine (10 microM-30 mM) but not glyceryl trinitrate (10 microM-1 mM) with catalase (1000 u ml-1) in the presence of hydrogen peroxide (1 mM) led to production of nitrite, a major breakdown product of nitric oxide. AT (1-100 mM) inhibited, in a concentration-dependent manner, the formation of nitrite from azide in the presence of hydrogen peroxide. 7. These data suggest that metabolism by catalase plays an important role in the relaxation induced by hydroxylamine and sodium azide in isolated rings of rat aorta. Relaxation appears to be due to formation of nitric oxide and activation of soluble guanylate cyclase. In contrast, metabolism by catalase does not appear to be involved in the relaxant actions of hydrogen peroxide or glyceryl trinitrate.

Amitrole↗
PubMedDate not supplied

Sodium azide burn: a case report.

Chemical burn injuries commonly occur at the workplace and can be caused by a variety of agents. Sodium azide is a volatile compound used in the industrial setting and it is also a constituent of car airbags. The known toxic effects of sodium azide include hypotension, bradycardia, and headaches. At the cellular level, it inhibits of ATP production by blocking the respiratory oxidation cascade. In the burn literature only one previous report documents a sodium azide hand burn caused by airbag malfunction. We report a case of massive exposure and resultant systemic toxicity from a sodium azide canister explosion.

Adult↗
PubMed1994

Some problems associated with measuring monoamine oxidase activity in the presence of sodium azide.

The colourimetric assay of monoamine oxidase activity, as hydrogen peroxide production, normally requires the use of sodium azide to inhibit breakdown of hydrogen peroxide by catalase. Sodium azide was shown to act as an uncompetitive inhibitor of benzylamine deamination with an inhibitor constant of 1.5 mM. Catalase activity of isolated rat liver mitochondria could be eliminated with the irreversible inhibitor of catalase, 3-amino-1,2,4-triazole. The treatment did not affect benzylamine deaminating activity. The catalase-free preparation could be used to assay monoamine oxidase activity colourimetrically, as hydrogen peroxide production, in the absence of sodium azide.

Amitrole↗
PubMed1991

Inhibition of lignin peroxidase H2 by sodium azide.

The oxidation of veratryl alcohol (3,4-dimethoxybenzyl alcohol) by lignin peroxidase H2 from Phanerochaete chrysosporium and H2O2 was strongly inhibited by sodium azide. Inhibition was competitive with respect to veratryl alcohol (Ki = 1-2 microM) and uncompetitive with respect to H2O2. In contrast, sodium azide bound to the native enzyme at pH 6.0 with an apparent dissociation constant (KD) of 126 mM. Formation of azidyl radicals was detected by ESR spin trapping techniques. The enzymes is nearly completely inactivated in four turnovers. The H2O2-activated enzyme intermediate (compound I) reacted with sodium azide to form a new species rather than be reduced to the enzyme intermediate compound II. The new species has absorption maxima at 418, 540, and 570 nm, suggesting the formation of a ferrous-lignin peroxidase-NO complex. Confirmation of this assignment was obtained by low-temperature ESR spectroscopy. An identical complex could be simulated by the addition of nitrite to the reduced enzyme. The enzyme intermediate compound II is readily reduced by sodium azide to native enzyme with essentially no loss of activity.

Agaricales↗
PubMed1994

Isolation and characterization of a Bacillus subtilis secA mutant allele conferring resistance to sodium azide.

A mutation has been isolated in the Bacillus subtilis secA gene (secA10) which allows cell growth and residual protein translocation in the presence of 1.5 mM sodium azide. Besides conferring resistance to sodium azide, the corresponding SecA10 mutant protein, in which glutamic acid at position 338 has been changed to glycine, seems to possess a secretion defect even in the absence of azide. In addition, the secA10 mutant protein was found to be recessive to wild-type secA with regard to azide resistance. Our results strongly suggest that, like the situation in Escherichia coli, the B. subtilis SecA protein is a main target for the lethal action of sodium azide.

Azides↗
PubMed1978

Effects of sodium azide on the quantitation of the chemical constituents of serum. Inhibition of bilirubin and cholesterol.

Azide salts frequently are added as a preservative to biologic fluids and reagents, or are introduced into serum through accidental exposure, intoxication, or pharmaceuticals. Sodium azide can interfere with the quantitation of biochemical constituents in serum. Serum pools containing 0.2-9.0 mg/dl (3.42-153.9 mumol/l) total bilirubin, 0.2-5.0 mg/dl (3.42-94.1 mumol/l) direct bilirubin, and 175-313 mg/dl (4.55-8.14 mmol/l) cholesterol were analyzed using the SMA 12/60. Sodium azide was added in concentrations of 0.1-1.0% (13.6-136 mmol/l). Sodium azide in concentrations of 0.1% (13.6 mmol/l) or more reduced total and direct bilirubin values 60-100%. At concentrations above 0.5% (68 mmol/l), no bilirubin, or only a very small quantity, was measured. Sodium azide at concentrations above 0.05% (6.8 mmol/l) exerted a significant decreasing effect on serum cholesterol values. At 0.1% (13.6 mmol/l) or more, reductions in cholesterol values ranging from 30 to 85% were observed. These studies showed that sodium azide (0.1%, 13.6 mmol/l, or more) in the serum can result in falsely low bilirubin or cholesterol values.

Alkaline Phosphatase↗
PubMed1995

Chronic sodium azide treatment decreases membrane-bound protein kinase C activity in the rat hippocampus.

Chronic administration of sodium azide in rats inhibits cytochrome oxidase and produces learning and memory deficits. The present experiment tested the hypothesis that chronic sodium azide treatment might also alter protein kinase C activation. Continuous infusion of sodium azide (400 micrograms/h, sc) in rats for 2 weeks significantly decreases membrane-bound protein kinase C in hippocampus, but not frontal cortex, temporal cortex, or cerebellum. Since protein kinase C activation is correlated with hippocampus-dependent learning, these results suggest a possible biochemical mechanism for azide-induced impairment of learning.

Animals↗
PubMed1996

Chronic in vivo sodium azide infusion induces selective and stable inhibition of cytochrome c oxidase.

The effect of chronic subcutaneous infusion of sodium azide on the activity of mitochondrial respiratory chain enzymes was investigated in Sprague-Dawley rats. Treatment with approximately 1 mg/kg/h sodium azide induced chronic, partial inhibition of cytochrome c oxidase, whereas the activities of respiratory complexes I and III were not significantly affected. The inhibition of cytochrome c oxidase was evident by 7 days after infusion began, and the effect was stable for at least 3 weeks. The selectivity of azide for cytochrome c oxidase is discussed in the context of other findings of azide effects on enzymes. The results of the present study indicate that the sodium azide infusion paradigm described here provides a useful tool for the evaluation of selective and stable cytochrome oxidase inhibition in vivo.

Analysis of Variance↗
PubMed1992

Low concentrations of sodium azide specifically inhibit a thromboxane A2 pathway in human platelets.

Sodium azide completely inhibits the serotonin release induced by ADP, arachidonic acid and the thromboxane A2 mimetic U46619, but does not have any effect on the activation by PMA. Collagen and thrombin are inhibited when used at low concentrations, but not at high concentration. This pattern of activation suggests that the inhibition by azide is not a metabolic inhibition. The antagonism of U46619-induced secretion was further studied and was shown to be non-competitive. It is selective for certain components of the U46619 stimulus-response coupling: aggregation, serotonin secretion and the activation of protein kinase C are completely or almost completely inhibited by 300 microM sodium azide. Shape change, calcium elevation, cytoplasmic alkalinization and phosphorylation of myosin light chain are only partially modified. This suggests that azide may specifically inhibit one of the different forms of thromboxane A2 receptors present in platelets.

Adenosine Diphosphate↗
PubMed2001

Intraocular pressure and vascular effects of sodium azide in bovine perfused eye.

The effects of the nitrovasodilator, sodium azide, on intraocular pressure (IOP) and ciliary vascular tone were compared. IOP was measured in the bovine isolated eye that was perfused via the ciliary artery. Separately, vasodilator effects were assessed after raising the vascular tone using noradrenaline (10 microM). Aqueous humor formation (AHF) rate was estimated by a fluorescein dilution method. Cyclic GMP in the ciliary processes was measured by radioimmunoassay. When compared with controls, sodium azide (10 nmole bolus dose) was found to lower IOP (2.2 +/- 0.3 mm Hg; P < 0.01) via a reduction in AHF (12.19 +/- 0.26 microl/min to 6.36 +/- 0.53 microl/min; P < 0.001). Azide (1 micromole) also reduced ciliary vascular resistance (81.0 +/- 5.5%; P < 0.01). However, the drug was 20x more potent as an ocular hypotensive than as a vasodilator (ED50 0.28 nmole on IOP, 5.55 nmole on vascular effect). Azide (10 nmole) also increased levels of ciliary cyclic GMP (127 +/- 17 fmol/mg protein to 233 +/- 27 fmol/mg protein; P < 0.01). The IOP-lowering effect of azide does not appear to depend on its ability to activate guanylyl cyclase (GC) in vascular smooth muscle, but rather is likely a consequence of direct activation of ciliary epithelial GC.

Animals↗
PubMedDate not supplied

[Effect of sodium azide on heat-shock resistance in Saccharomyces cerevisiae and Debaryomyces vanriji yeasts].

The pretreatment of Saccharomyces cerevisiae and Debaryomyces vanriji with sodium azide was found to induce thermotolerance in both yeasts, whereas sodium azide used in combination with heat shock enhanced the thermotolerance of S. cerevisiae and substantially decreased the thermotolerance of D. vanriji. It is suggested that the different responses of the yeasts to sodium azide during heat shock are due to the different functional organizations of their mitochondrial apparatus.

Adaptation, Physiological↗
PubMed1979

Mutagenesis of Saccharomyces cerevisiae by sodium azide activated in barley.

Concentrated dialysate of the extract prepared from barley seeds treated with sodium azide increased up to 100--200 times the frequency of forward mutations to cycloheximide resistance in the excision-deficient UV-sensitive heploid strain rad2-5 of Saccharomyces cerevisiae, when applied to growing cells in complete medium at pH 4.2. Only a slight increase of mutation frequency (less than 4 times) was found in the haploid RAD+ strain treated in the same way as well as in haploid RAD+ and rad2-5 strains treated directly by sodium azide. In contrast with the barley-activated sodium azide, UV irradiation was more effective in the induction of cycloheximide resistance in the RAD+ strain than in the RAD2-5 mutant. The dialysate from azide-treated barley seeds, applied at both pH 4.2 and pH 9, also significantly increased the frequency of locus-specific suppressor mutations to isoleucine independence and -- to a lesser extent -- reversions and/or gene conversions in the trp5 locus in growing cells of the diploid strain D7. The dialysate was also mutagenic in resting cells of strains D7 and rad2-5 but with lower effectiveness.

Azides↗
PubMed1989

Differential metabolism of sodium azide in maize callus and germinating embryos.

Sodium azide is a potent mutagen of maize (Zea mays L.) kernels that may have potential as a point mutagen for inducing biochemical mutations in maize tissue cultures. Azide mutagenicity was evaluated in friable, embryogenic maize callus and a nonregenerable maize suspension culture by determining the number of resistant variant cell lines able to grow on media containing inhibitory concentrations of lysine plus threonine (LT). The number of LT-resistant variants selected from either culture type did not increase in response to azide treatment. In addition, there was no increase in somatic mutations in more than 100 plants regenerated from azide treated LT-resistant lines. The levels of mutagenic metabolite of azide (presumably azidoalanine), were determined by bioassay in the two azide-treated maize callus types and compared to levels of mutagenic metabolite in embryos isolated from azide-treated kernels. The two types of maize tissue cultures and isolated embryos contained similar levels of mutagenic metabolite 4 h after azide treatment indicating similar uptake and conversion of azide to mutagenic metabolite in the three tissues. Mutagenic metabolite in azide-treated embryos did not significantly decrease after 40 h. However, mutagenic metabolite levels in both azide-treated tissue cultures decreased to near background levels within 20 h providing evidence for rapid metabolism of the azide mutagenic metabolite. The lack of evidence for azide mutagenicity in maize callus and its known potent mutagenicity in kernels appears to be associated with specific differences in azide metabolism between callus tissues and kernel embryos.

Azides↗