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PubMed2001

Opening of thiiranes: preparation of orthogonal protected 2-thioglyceraldehyde.

Treatment of acrolein diethyl acetal sulfide 8 with methanesulfenyl bromide at low temperature results in an efficient thiirane ring opening to a halo disulfide 9. The bromine in this halo disulfide is easily substituted by silver acetate, sodium azide, sodium iodide, and silver nitrate. Treatment of 9 with tetrabutylammonium acetate yields a novel dehydrohalogenation product 12. Silica gel converts bromide 9 into a disulfide-substituted version of acrolein 15. The orthogonal-protected version of 2-thioglyceraldehyde 13 can be deprotected to a useful form of this aldehyde.

Glyceraldehyde↗
PubMed2006

Aziridinium from N,N-dibenzyl serine methyl ester: synthesis of enantiomerically pure beta-amino and alpha,beta-diamino esters.

[reaction: see text] Reaction of N,N-dibenzyl-O-methylsulfonyl serine methyl ester with a variety of heteronucleophiles (sodium azide, sodium phthalimide, amines, thiols) and carbanions (sodium malonate) gave, via an aziridinium intermediate, the corresponding beta-amino or alpha,beta-diamino ester in good to excellent yield. A short synthesis of orthogonally protected and enantiomerically pure 2,3-diamino propionate (Dap) is described.

Aziridines↗
PubMed2001

B-subunit of phosphate-specific transporter from Mycobacterium tuberculosis is a thermostable ATPase.

The B-subunit of phosphate-specific transporter (PstB) is an ABC protein. pstB was polymerase chain reaction-amplified from Mycobacterium tuberculosis and overexpressed in Escherichia coli. The overexpressed protein was found to be in inclusion bodies. The protein was solubilized using 1.5% N-lauroylsarcosine and was purified by gel permeation chromatography. The molecular mass of the protein was approximately 31 kDa. The eluted protein showed ATP-binding ability and exhibited ATPase activity. Among different nucleotide triphosphates, ATP was found to be the preferred substrate for M. tuberculosis PstB-ATPase. The study of the kinetics of ATP hydrolysis yielded K(m) of approximately 72 microm and V(max) of approximately 0.12 micromol/min/mg of protein. Divalent cation like manganese was inhibitory to the ATPase activity. Magnesium or calcium, on the other hand, had no influence on the functionality of the enzyme. The classical ATPase inhibitors like sodium azide, sodium vanadate, and N-ethylmaleimide were without any effect but an ATP analogue, 5'-p-fluorosulfonylbenzoyl adenosine, inhibited the ATPase function of the recombinant protein with a K(i) of approximately 0.40 mm. Furthermore, there was hardly any ATP hydrolyzing ability of the PstB as a result of mutation of the conserved aspartic acid residue to lysine in the Walker motif B, confirming the recombinant protein is an ATPase. Interestingly, analysis of the recombinant PstB revealed that it is a thermostable ATPase; thus, our results highlight for the first time the presence of such an enzyme in any mesophilic bacteria.

ATP-Binding Cassette Transporters↗
PubMed1981

Monocyte-mediated serum-independent damage to hyphal and pseudohyphal forms of Candida albicans in vitro.

Human peripheral blood monocytes attached to Candida albicans hyphae in the absence of serum and damaged the hyphae without completely ingesting them. Attachment and damage was not augmented by the addition of serum. Damage to hyphae was quantitated by a previously developed metabolic assay that measured leukocyte-induced reduction in uptake of [(14)C]cytosine by the hyphae. Use of cells from patients with hereditary disorders of leukocyte function, chronic granulomatous disease, and myeloperoxidase deficiency indicated that myeloperoxidase-independent and nonoxidative mechanisms could sometimes damage hyphae where oxidative mechanisms were impaired. Damage to hyphae by normal monocytes was inhibited by concentrations of sodium azide and sodium cyanide that primarily affect myeloperoxidase activity, as well as by halide-free conditions, catalase, and putative antagonists of hypochlorous acid or singlet oxygen. Iodination of hyphae, a myeloperoxidase and hydrogen peroxide-dependent process of monocytes, was similarly inhibited by sodium azide, sodium cyanide, and catalase. Under anaerobic conditions, damage to hyphae was reduced by 64.0-68.4%. In contrast, inhibitors of potential nonoxidative antifungal mechanisms, iron salts to saturate iron chelators, and polyanionic amino acid polymers to neutralize cationic proteins did not block damage to hyphae by monocytes. Preparations rich in lysosomal granules from fractionated normal monocytes also did not damage hyphae. Overall, it appeared that oxidative mechanisms were most important for damage to hyphae by normal monocytes. Electron microscopy confirmed that Candida hyphae were damaged and probably killed by monocytes, but monocytes appeared to sustain significant damage in the process. In the absence of serum, monocyte cell membranes became closely approximated to Candida cell walls. It appeared that some Candida could escape this partial engulfment, as they were seen floating free with vesicular trilaminar membrane remnants covering hyphal surfaces. In general, monocytes appeared to be damaged by interactions with Candida hyphae more than neutrophils had been in previous studies.

Candida albicans↗
PubMed2006

Characterization of monofunctional catalase KatA from radioresistant bacterium Deinococcus radiodurans.

Catalase plays a key role in protecting cells against toxic reactive oxygen species. Here we report on the cloning, purification and characterization of a catalase (KatA, DR1998) from the extremely radioresistant bacterium Deinococcus radiodurans. The size of purified D. radiodurans KatA monomer was 65 kDa while gel filtration revealed that the size of the enzyme was 240 kDa, suggesting that KatA formed a homotetramer in solution. Purified KatA displayed a final specific activity of 68,800 U/mg of protein. The catalase activity of KatA was inhibited by sodium azide, sodium cyanide and 3-amino-1,2,4-triazole. The absorption spectrum of KatA exhibited a Soret band at 408 nm. The position of the spectral peak remained unchanged following reduction of KatA with dithionite. No peroxidase activity was found for KatA. These results demonstrate that D. radiodurans KatA is a typical monofunctional heme-containing catalase. The stability of KatA with respect to H2O2 stress was superior to that of commercially available Aspergillus niger and bovine liver catalases. The relative abundance of KatA in cells in addition to the H2O2 resistance property may play a role in the survival strategy of D. radiodurans against oxidative damage.

Amino Acid Sequence↗
PubMed1991

[The specific characteristics of the vertebrate electroretinogram evoked by x-rays].

Summarised electroretinograms (ERGs) of dark-adaptable retina of Rana temporaria were studied in situ with an automated experimental device with programmable control and first and second derivatives electron differentiation. X-rays were shown to induce the ERG composed of two components which were conventionally designated as the first and second roentgen responses (R-1 and R-2). These differ by their parameters from the ERGs induced by red and blue light in the same experiment. Administration of sodium azide, sodium nitrite, monoiodine acetate and other compounds changed the waves of R-1 and R-2 as well as photo-induced ERGs. This suggests their relative independence and different mechanism of initiation, and allows their partial isolation for separate studying.

Animals↗
PubMed1976

[Study of betacyanin-discolorating enzyme].

An enzyme catalyzing the discoloration and breakdown of betacyanins was isolated from beet roots Beta vulgaris by centrifugation in sucrose density gradient (2.5 M, 2.0 M, 1.5 M, 1.0 M, tris-HCl buffer, 0.05 M, pH 7.2), and purified 100-fold. The enzyme activity induced the discoloration of betanin, betanidin. It was found that the beet root enzyme exists in an insoluble state and is firmly bound with subcellular structures, which were isolated by centrifugation in sucrose gradient. The optimal activity of the enzyme was observed at pH 3.4, +40 degrees C. The dependence of the enzymatic reaction on the enzyme concentration showed a linearity. Studies of the enzyme inhibition by sodium azide, sodium diethyldithiocarbamate, thiourea, demonstrated that the active site of the enzyme contains a metal. The enzymatic discoloration of betanin is followed by the oxygen uptake.

Centrifugation, Density Gradient↗
PubMedDate not supplied

[Mechanism of NADH-sensitized formation of DNA breaks during irradiation with near UV light].

NADH-photosensitized in vitro formation of single-stranded breaks in plasmid DNA pBR322 depends on both the concentration of the sensitizer and the influence of near-UV radiation (320-400 nm). Scavengers and inhibitors of different activated oxygen species (sodium azide, sodium benzoate, catalase and superoxide dismutase) prevent the formation of breaks in full or partly. The data obtained show that hydroxyl radical (.OH) and singlet oxygen (1O2) are directly involved in the induction of breaks. In this process hydrogen peroxide (H2O2) plays the role of an intermediate in the reaction of .OH formation from superoxide anion-radical (O2-.) which is the first NAD.H-photogenerated product.

DNA Damage↗
PubMed1987

Neutrophil-mediated cytotoxicity triggered by immune complexes: the role of reactive oxygen metabolites.

Normal human neutrophils triggered by precipitating immune complexes (IC), soluble IC (sIC) or heat-aggregated IgG (HAIgG) displayed low levels of cytotoxicity towards nonsensitized target cells. Catalase, but not heated catalase, completely impaired this nonspecific cytotoxicity (NSC), suggesting a key role for hydrogen peroxide (H2O2) in the lysis of target cells. Superoxide dismutase (SOD) and certain HO. and 1O2 scavengers were unable to exert significant effects. Three haem-enzyme inhibitors, sodium azide, sodium cyanide and 3-amino-1,2,4-triazole did not decrease neutrophil NSC, but markedly enhanced it. This data suggest that the mechanism involved was not dependent upon myeloperoxidase (MPO). The analysis of neutrophil-mediated ADCC indicates that oxygen-dependent but MPO-independent mechanisms appeared to be operative in this system. It was also found that the microfilament disrupting agents, cytochalasin B (CB) and dihydrocytochalasin B (dhCB), as well as the chemotactic peptide N-formyl-methionyl-leucyl-phenylalanine (FMLP), significantly enhanced NSC. In contrast, these compounds partially inhibited ADCC. This cytotoxic system provides a suitable model to study events that may occur during the course of immune complex diseases and also permits the evaluation of alternative lytic mechanisms triggered through neutrophil Fc gamma receptors.

Antibody-Dependent Cell Cytotoxicity↗
PubMed1985

Purification and properties of H+-translocating, Mg2+-adenosine triphosphatase from vacuolar membranes of Saccharomyces cerevisiae.

H+-translocating, Mg2+-ATPase was solubilized from vacuolar membranes of Saccharomyces cerevisiae with the zwitterionic detergent N-tetradecyl-N,N-dimethyl-3-ammonio-1-propanesulfonate and purified by glycerol density gradient centrifugation. Partially purified vacuolar membrane H+-ATPase, which had a specific activity of 18 units/mg of protein, was separated almost completely from acid phosphatase and alkaline phosphatase. The purified enzyme required phospholipids for maximal activity and hydrolyzed ATP, GTP, UTP, and CTP, with this order of preference. Its Km value for Mg2+-ATP was determined to be 0.21 mM and its optimal pH was 6.9. ADP inhibited the enzyme activity competitively, with a Ki value of 0.31 mM. The activity of purified ATPase was strongly inhibited by N,N'-dicyclohexylcarbodiimide, 1-ethyl-3-(3-dimethylaminopropyl)carbodiimide, tributyltin, 7-chloro-4-nitrobenzoxazole, diethylstilbestrol, and quercetin, but was not affected by oligomycin, sodium azide, sodium vanadate, or miconazole. It was not inhibited at all by antiserum against mitochondrial F1-ATPase or mitochondrial F1-ATPase inhibitor protein. These results indicated that vacuolar membrane H+-ATPase is different from either yeast plasma membrane H+-ATPase or mitochondrial F1-ATPase. The vacuolar membrane H+-ATPase was found to be composed of two major polypeptides a and b of Mr = 89,000 and 64,000, respectively, and a N,N'-dicyclohexylcarbodiimide binding polypeptide c of Mr = 19,500, whose polypeptide composition was also different from those of either plasma membrane H+-ATPase or mitochondrial F1-ATPase of S. cerevisiae.

Adenosine Triphosphate↗
PubMed1982

A ganglioside-dependent cellular binding mechanism in rat macrophages.

A rosetting assay was performed with rat alveolar and peritoneal macrophages and sheep red blood cells (SRBC) treated with gangliosides. SRBC incubated with GM2, GD1a, and a mixture of bovine brain gangliosides (BBG) showed binding to rat macrophages. The extent of binding was dependent on the concentration of gangliosides. Binding induced by GM2 was stronger than that induced GD1a and BBG. GM1 and GA2 did not induce rosette formation. Inhibition studies with gangliosides, sialyllactose, lactose, and neuraminic acid suggested that the macrophage binding site recognizes neuraminic acid in conjunction with neighboring carbohydrates showing highest affinity for GM2. Sodium azide, sodium fluoride, ethylenediaminetetraacetate, cytochalasin B, and colchicine did not inhibit rosette formation. The percentage of peritoneal macrophages binding ganglioside-treated SRBC was lower than that of alveolar macrophages. Proteose-peptone-stimulated peritoneal macrophages, however, showed an increase of rosette formation. Around 30% of adherent spleen cells also had binding activity for GM2-treated SRBC. Peripheral blood mononuclear cells did not bind ganglioside-treated SRBC. Phagocytosis of GM2-treated SRBC attached to alveolar macrophages could not be observed. It is suggested that macrophages may express recognition sites for certain gangliosides that might be important in cell-cell interaction.

Animals↗
PubMed2001

Effect of the respiratory activity on photoinhibition of the cyanobacterium Synechocystis sp.

The influence of respiratory activity on photosynthesis in Synechocystis cells that had been exposed to high light intensity was studied using distinct conditions of nitrogen supply. The photoinhibitory rate of N-sufficient cells was not influenced by the presence of different nitrogen sources. In contrast, when N-starved cells were resupplied with ammonium, they were protected from photoinhibition. Although N-starved cells presented a higher rate of dark O(2) uptake than N-sufficient ones, the photoinhibitory rate increased in both cases after addition of sodium azide or sodium azide plus salicylhydroxamic acid in the photoinhibitory treatment. In the absence of the D(1) protein repair mechanism, photodamage to Photosystem II was faster in N-sufficient cells than in N-starved ones. Mitigation of photodamage disappeared when the respiratory activity of N-starved cells was partially suppressed by the addition of sodium azide or sodium azide and salicylhydroxamic acid. Our results suggest that electron flow through cyanobacterial terminal oxidases can assist Photosystem I in removing electrons from the reduced plastoquinone pool, thus contributing to both reopening of Photosystem II reaction centers and avoiding photogeneration of reactive oxygen species under photoinhibitory conditions.

Journal Article↗
PubMed1985

Photometric analysis of antifading reagents for immunofluorescence with laser and conventional illumination sources.

Bleaching of stained objects is a major problem in immunofluorescence. The prevention of fluorescence fading would allow longer observation times, photographic documentation, fluorometry, and pattern recognition. Fluorescein kinetics and fluorescence intensities (FI) of fluorescein isothiocyanate (FITC) conjugate-stained Sephadex beads were studied with previously described "antibleaching" reagents using an argon laser as the excitation light source. Eight antibleaching reagents were tested (sodium azide (NaN3), sodium iodide (NaI), polyvinyl pyrrolidone (PVP), polyvinyl alcohol (PVA), 1,4-di-azobicyclo-(2,2,2)-octane (DABCO), p-phenylenediamine (PPD), n-propylgallate, and sodium dithionite (Na2S2O4]. Sodium azide and sodium iodide were found to increase FI. This was likewise found with mercury arc illumination and hence they may prove useful for routine immunofluorescence tests. PPD was found to accumulate on the surface of the beads and to disturb immunofluorescence by autofluorescence. The value of any of the other reagents in immunofluorescence is questionable.

Argon↗
PubMed1979

Sodium azide-induced mutagenesis in Saccharomyces cerevisiae.

Sodium azide (0.5--2.0 X 10(-5) M), applied for 24 h on cells growing in complete medium, increased up to 26 times the frequency of reversions and locus-specific suppressor mutations of allele ilv1-92 in diploid strain D7 of Saccharomyces cerevisiae. Similarly, it enhanced the frequency of reversions and/or mitotic gene conversions of alleles trp5-12/trp5-27 up to 19 times. Reconstruction experiments showed that the increase of mutations in complete medium was not due to a selection of prototrophic types under growth conditions and, therefore, that sodium azide acts as a weak mutagen in S. cerevisiae under growth conditions at a low pH. No mutagenic or convertogenic effect was observed when azide was applied to resting cells in buffer at pH 4.2.

Azides↗
PubMed1998

Restoration of the activity of active-site mutants of the hyperthermophilic beta-glycosidase from Sulfolobus solfataricus: dependence of the mechanism on the action of external nucleophiles.

The beta-glycosidase from the hyperthermophilic Archaeon Sulfolobus solfataricus hydrolyzes beta-glycosides following a retaining mechanism based upon the action of two amino acids: Glu387, which acts as the nucleophile of the reaction, and Glu206, which acts as the general acid/base catalyst. The activities of inactive mutants of the catalytic nucleophile Glu387Ala/Gly were restored by externally added nucleophiles. Sodium azide and sodium formate were used as external nucleophiles and the products of their reaction were characterized. Glu387Ala/Gly mutants were reactivated with 2, 4-DNP-beta-Glc substrate and the Glu387Gly mutant showed recovered activity, with the same nucleophiles, also on 2-NP-beta-Glc. The reaction catalyzed by the Glu387Gly mutant proceeded differently depending on the type of externally added nucleophile. Sodium azide restored the catalytic activity of the mutant by attacking the alpha-side of the anomeric carbon of the substrates, thereby yielding an inverting glycosidase. Sodium formate promoted the opposite behavior (retaining) in the mutant, producing 3-O-beta-linked disaccharide derivative of the substrates. A possible role of sodium formate as a biomimicking agent in replacing the natural nucleophile Glu387 is also discussed.

Binding Sites↗
PubMed2002

Bacterial adhesion onto azidated poly(vinyl chloride) surfaces.

A plasticized poly(vinyl chloride) surface was modified by azidation using sodium azide in the presence of a phase transfer catalyst in aqueous media. Subsequent to azidation, the surface was crosslinked using ultraviolet radiation. Contact angle measurements showed that the surface became hydrophilic on azidation whereas photoirradiation did not have any further effect on the hydrophilicity of the azidated surface. Control, azidated, and photocrosslinked surfaces were exposed to two strains of bacteria commonly implicated in device infection such as Staphylococcus aureus and Escherichia coli. Whereas the control and photocrosslinked surfaces showed no significant difference in bacterial adhesion, the azidated surface showed significantly reduced adhesion to both strains. Data obtained indicate that the presence of an intact azide function on the polymer surface is responsible for the reduced bacterial adherence and the surface hydrophobicity/hydrophilicity did not exert any effect in the present case. Although azides are known to be effective only against Gram-negative species, surprising was the observation that the azidated polymer surface was equally effective against a Gram-positive species such as S. aureus. Because sodium azide is routinely used as a preservative to prevent bacterial and fungal growth in many microbiology reagents and diagnostic kits, covalent binding of the azide onto a polymer surface or synthesizing azide containing polymers may be an interesting method to investigate in tackling the problem of bacterial adhesion and colonization of medical devices.

Azides↗
PubMed2004

Burn injuries resulting from (accidental) airbag inflation.

INTRODUCTION: Airbags are intended to minimize facial injuries, alone and when used in combination with seatbelts in high-velocity motor-vehicle accidents. They may occasionally perforate, resulting in the release of sodium azide or sodium hydroxide, which result in chemical burns when in contact with skin. The force of deployment may itself result in significant blunt trauma, and there is a temperature rise during the inflation causing thermal burns, possibly as a separate and unnecessary consequence of a relatively minor accident. METHOD: A case report is presented. The literature on such injuries was reviewed and the mechanism of airbag deployment commented. CONCLUSION: Alternative designs and mechanisms of linking the activation of the device to the velocity of travel or to add a switch which is activated when accessing a motorway are recommended.

Aged↗
PubMed2003

Transport of 5-formyltetrahydrofolate into primary cultured cerebellar granule cells.

Transport of 5-formyltetrahydrofolate (5-FTHF) into primary cultured cerebellar granule cells (CGC) was studied. Uptake of 5-FTHF into CGC was saturable with K(m)=2.86 microM and V(max)=40.8 pmol/mg protein/45 min in pH 7.4 medium. Uptake of 5-FTHF in the astrocytes has a similar style in the time curve. Uptake of 5-FTHF is characterized by countertransport because adding unlabeled 5-FTHF in the medium resulted in the efflux of labeled 5-FTHF. Uptake of 5-FTHF was inhibited by the structural analogs 5-methyltetrahydrofolate, methotrexate and folic acid (K(i)=6.64, 7.69, and 19.38 microM, respectively). Uptake was significantly decreased by high concentrations of sodium azide and sodium arsenate but not by sodium cyanide. Uptake was also inhibited by p-chloromercuriphenylsulfonate and by the anions probenecid and 4,4'-diisothiocyanostilbene-2,2'-disulfonic acid. Acute exposure of the cells to ethanol (100 mM) did not affect the uptake. It is concluded that CGC have a carrier-mediated system for the uptake of 5-FTHF and other folates.

Animals↗