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[Several features of the antioxidant action of chemical carcinogens].

Comparative studies of antioxidative effects of phenole inhibitors (vitamine E) amino-and sulfur-containing radioprotectors, and chemical cancerogens on oxidation of unsatured fatty acid were carried out. Some polycyclic hydrocarbons and azo-compounds produce a prolonged and stable decrease of peroxide accumulation rate in oxidized oleic acid. Due to this property in the in vivo systems chemical cancerogenes can induce prolonged stable changes in the parameters of vitally important redox processes.

9,10-Dimethyl-1,2-benzanthracene↗
PubMed1976

[A contribution to the identification of the oral antidiabetic agent tolbutamide. 1st communication].

An identification reaction for tolbutamide given in several pharmacopoeias involves the reaction of n-butylamine, formed by acid hydrolysis of tolbutamide, with diazotised p-nitroaniline to yield a characteristic red colour of unknown structure(s). It is demonstrated that, by using TLC methods, this red colour can be separated into 8 red or yellow coloured components. The structures of these isolated compounds were determined by spectroscopical methods and, in six cases, confirmed by unequivocal synthesis. These coloured components include one pentazdiene, five triazenes and two nitro compounds.

Aniline Compounds↗
PubMed2003

Differential inhibitory action of two azoic compounds against arenaviruses.

The action of five azo-based compounds against the arenaviruses Junin (JUNV) and Tacaribe (TCRV) was evaluated in vitro by a virus yield inhibition assay in Vero cells and a cell-free virion inactivation assay. The compound 2-azo-(1'-(2'-nitroso)naphthyl)-benzoate (ANNB) was the most effective inhibitor of arenavirus production in Vero cells with EC(50) (effective concentration 50%) values in the range 6.5-26.2 microM and without inactivating properties. By contrast, the azodicarbonamide (ADA) was very effective in inactivating both arenaviruses with IC(50) (inactivating concentration 50%) values of 7.6 and 5.3 microM against JUNV and TCRV, respectively. The virucidal activity of ADA was time- and temperature-dependent. ANNB had no inhibitory action on virus binding or penetration of target cells and did not affect the synthesis of viral proteins. The most likely event susceptible to ANNB would be the process of intracellular virion assembly.

Animals↗
PubMed2003

UV/Vis, IR and 1H NMR spectroscopic studies of bisazo-dianil compounds based on 5-(2-carboxyphenyl azo)-salicylaldehyde and primary diamines.

The electronic absorption and emission spectra of the titled biazo-dianils are studied in organic solvents of different polarity as well as in aqueous buffer solutions of varying pH. The important bands in the IR spectra as well as the main signals of the 1H NMR spectra are assigned. The observed UV/Vis absorption bands are assigned to the corresponding electronic transitions. The fluorescence quantum yield and pK(a)(-) values in the ground and excited states are determined.

Aldehydes↗
PubMed1995

Reduction of azo dyes and nitroaromatic compounds by bacterial enzymes from the human intestinal tract.

Several anaerobic bacteria from the human intestinal tract are capable of reducing azo dyes and nitropolycyclic aromatic hydrocarbons to the corresponding aromatic amines with enzymes that have azoreductase and nitroreductase activities. The majority of bacteria with these activities belong to the genera Clostridium and Eubacterium. The azoreductases and nitroreductases from three Clostridium strains and one Eubacterium strain were studied. Both enzymes were produced constitutively in each of the bacteria; the enzymes from various bacteria had different electrophoretic mobilities. The azoreductases from all of the bacteria had immunological homology, as was evident from the cross-reactivity of an antibody raised against the azoreductase of C. perfringens with azoreductases from other bacteria. Comparison of azoreductases and nitroreductases showed that they both had identical electrophoretic mobilities on polyacrylamide gels and reacted with the antibody against the azoreductase from C. perfringens. Furthermore, the nitroaromatic compounds competitively inhibited the azoreductase activity. The data indicate that the reduction of both nitroaromatic compounds and azo dyes may be carried out by the same enzyme, which is possibly a flavin adenine dinucleotide dehydrogenase that is synthesized throughout the cell and not associated with any organized subcellular structure.

Azo Compounds↗
PubMed1989

Photo-oxidation of sulphanilamide to azo and azoxy compounds.

The second-order kinetics for the photochemical formation of azobenzene-4, 4-disulphonamide has been studied at pH 1-11 and at pH 7.0 in the presence of five antioxidants. The rate constants are not affected by changes in pH in the region of 5-9 at which the molecule is predominantly in the unionised form. The rate of formation of azobenzene-4, 4'-disulphonamide is inhibited upto 80% by ascorbic acid. A scheme for the photo-oxidation of sulphanilamide to the azo and azoxy derivatives has been outlined.

Journal Article↗
PubMed2006

Binding properties of HABA-type azo derivatives to avidin and avidin-related protein 4.

The chicken genome encodes several biotin-binding proteins, including avidin and avidin-related protein 4 (AVR4). In addition to D-biotin, avidin binds an azo dye compound, 4-hydroxyazobenzene-2-carboxylic acid (HABA), but the HABA-binding properties of AVR4 are not yet known. Differential scanning calorimetry, UV/visible spectroscopy, and molecular modeling were used to analyze the binding of 15 azo molecules to avidin and AVR4. Significant differences are seen in azo compound preferences for the two proteins, emphasizing the importance of the loop between strands beta3 and beta4 for azo ligand recognition; information on these loops is provided by the high-resolution (1.5 A) X-ray structure for avidin reported here. These results may be valuable in designing improved tools for avidin-based life science and nanobiotechnology applications.

Animals↗
PubMed2003

Mechanism-based invention of high-speed living radical polymerization using organotellurium compounds and azo-initiators.

Kinetic analysis reveals the existence of two competing pathways in the organotellurium-mediated living radical polymerization (TERP) at elevated temperature. The rate-determining step, namely, the thermal dissociation process, could be bypassed by the addition of conventional radical initiators, and the polymerization proceeded at low temperature by the degenerative transfer-mediated polymerization. The polymerization conditions are applicable to a variety of vinyl monomers, and the desired polymers form in a highly controlled manner.

Journal Article↗