[Effect of ultraviolet radiation as a sterilizing agent on synthetic dyes used in Poland for drug coloring. I. Azo dyes--derivatives of sulfanilic acid].
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Azo Compounds↗
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Results for “Sulfanilic Acids”
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[Coupling reaction of estradiol with diazotized sulfanilic acid].
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Benzenesulfonates↗
[Effect of tetracycline and some pharmaceutical adjuvants on the capillary and the lymphatic transport of sulfanilic acid from the rat small intestine].
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Adjuvants, Pharmaceutic↗
[Microflora of active ooze participating in the decomposition of sulfanilic acid].
Microflora of domestic water can be a source of active ooze adapted to sulphanilic acid. Adaptation of the microflora to sulphanilic acid at a concentration of 170-200 mg/l takes 6 to 8 days. The microflora of active ooze, immediately after adaptation, consists mainly of Pseudomonas species, Ps. denitrificans, Ps. fluorescens, Ps. striata, Ps. putida, etc., and also of Achromobacter stutzeri, Achromobacter flavum, Mycobacterium phlei, Mycobacterium mucosum, Bacillus mesentericus, Bac. cereus, saccharomyces cerevisiae, Schizosaccharomyces pombe, and Rhodotorula glutinus. The number of the species decreased as a result of long cultivation of active ooze on a minimal medium with sulphanilic acid as a sole source of carbon and nitrogen; the following strains prevailed: Ps. putida, Ps. eisenbergii, strains of Mycobacterium phlei and Flavobacterium solare. The isolated strains of Ps. putida and Ps. eisenbergii decomposed sulphanilic acid by 60.0--79.5 percent, and together with Mycobacterium phlei by 100 percent during 4 to 7 days. The ability to oxidize sulphanilic acid decreased after storage. Addition to the medium of other sources of carbon, nitrogen and vitamins did not restore the lost ability of the microorganisms to decompose sulphanilic acid.
Alcaligenes↗
Synthesis of diazotized 35S sulfanilic acid of high specific activity: a label for the outer surface of cell membranes.
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Animals↗
Effect of thiocyanate on nitrite estimation and the cleavage of nitrosamines.
Thiocyanate or bromide increased the colour formed by nitrite reacting with sulfanilic acid and naphthylethylenediamine. If the colour reagents were added together with thiocyanate (final concentration, M/10), the colour intensity was doubled. If sulfanilic acid was added three minutes before addition of naphthylethylenediamine, the relationship between nitrite concentration and colour production was more linear in the presence of thiocyanate. This effect was due to thiocyanate catalysing the diazotization of sulfanilic acid and inhibiting the reaction of nitrite with naphthylethylenediamine. Bromide and thiocyanate are similar in their catalytic effects on nitrosation, and hydrobromic acid in glacial acetic acid is an effective reagent for denitrosation of nitrosamine. Although thiocyanate catalysed denitrosation of nitrosamines, the effect was small except with nitrosomethylaniline, which had also been found to be denitrosated by sulfanilic acid. Thiocyanate could not be used generally for the destruction of nitrosamines; it was also found to be ineffective as an alternative to hydrobromic acid in the estimation of nitrosamines.
Acetates↗
Chemical treatment of macrophages increases their responsiveness to migration inhibitory factor (MIF).
The response of guinea pig macrophages to migration inhibitory factor (MIF) is altered by several chemical treatments. Treatment of macrophages with the diazonium salt of sulfanilic acid (5 x 10(-6) to 4 x 10(-4) M) significantly increases the response of these cells to MIF. Treatment with acetic anhydride also augments the response of these cells to MIF. The latter finding suggests that alteration of amino, hydroxyl, or sulfhydryl groups is involved in this phenomenon. Treatment of macrophages with sodium periodate (2 x 10(-5) to 10(-3) M) which is known to oxidize cis-glycols and with hydroxylamine (2 x 10(-5) to 2 x 10(-3) M), which reacts with carbonyl groups also increases response to MIF. The following experiments suggest that the significant alteration occurs at the level of the cell surface. Incubation of macrophages with the diazonium salt of sulfanilic acid at 4 degrees C, at which temperature pinocytosis is largely inhibited, is sufficient to increase the MIF response. The activity of the cytoplasmic enzyme aspartate aminotransferase, which in homogenates is susceptible to inactivation by low concentrations of the diazonium salt of sulfanilic acid, is not decreased when intact macrophages are incubated with high concentrations of the diazonium salt of sulfanilic acid. Cumulatively, these findings suggest that modification of different functional groups on the macrophage surface causes the same physiologic effect.
Anhydrides↗
Kinetics of the reactions of unconjugated and conjugated bilirubins with p-diazobenzenesulfonic acid.
We report the kinetics of the reactions of unconjugated bilirubin and conjugated bilirubin with p-diazobenzene sulfonic acid in aqueous media. Our studies confirm that each reaction proceeds in two steps and that the second step is catalyzed by sulfanilic acid. In the presence of an excess of p-diazobenzenesulfonic acid and in the absence of sulfanilic acid, the reaction for either unconjugated or conjugated bilirubin proceeds in two successive first-order steps, the second step being much the slower. This study emphasizes the first step in the reaction for each species and includes data on the effects of p-diazobenzenesulfonic acid, albumin, benzoate, and caffeine concentrations, pH in the range from 4 to 12, and temperature. Mechanisms proposed for reactions with and without caffeine are used to develop rate equations, and the kinetic data are used to evaluate rate constants, acid dissociation constants for the different bilirubin species, and formation constants for bilirubin-caffeine complex species that are proposed.
Azo Compounds↗
Fluorometric determination of nitrite in cured meats.
An indirect fluorometric method for determining sodium nitrite in meat products is presented. The extracted sodium nitrite is consumed in a diazotization reaction with a measured excess of sulfanilic acid. Fluorescamine, which acts selectively with primary amines such as sulfanilic acid, is a fluorogenic reagent for the excess amine. The amine consumed, calculated by difference from the total originally present, is directly related to the sodium nitrite content of the sample. Interferences from amino acids and soluble proteins in the meat extract are eliminated by judicious use of a secondary peak in the fluorescence spectra (436 nm excitation, 495 nm fluorescence) combined with measurement at low pH (3.30). The recoveries of sodium nitrite ranged from 83.2 to 99.6% with an average of 93.4 and a standard deviation of +/- 5.28% for 11 determinations.
Food Additives↗
The determination of the myocardial extracellular space in the cat in vivo: a comparative methodological study.
The myocardial extracellular space (ECS) was determined in cats in vivo by means of the ECS indicators, inulin and sulfanilic acid and, additionally, as glucose space. Experiments were carried out in cats subjected to bilateral kidney ligation (single injection) and in intact cats (single injection or infusion of indicator). The heart was clamped by instant deep-freezing in situ; this technique was compared, in renally-ligated cats, with excision and subsequent freezing of the heart in liquid nitrogen. The myocardial blood content was significantly decreased, and the myocardial lactate concentration significantly increased in excised, as compared with in situ-clamped hearts. Renally-ligated cats showed marked hypotension. The mean myocardial blood content was also significantly lower than in intact animals. A highly significant correlation was found between myocardial blood content and blood pressure for all experiments with instant deep-freezing. The mean inulin ECS value in renally-ligated cats was 22.7 +/- 1.5 ml. In accordance with the fact that the ECS is dependent on the tissure blood content, the corresponding values in intact animals were significantly higher, 25.9 +/- 2.5 ml (single injection) and 26.3 +/- 3.9 ml (infusion), calculated per 100 g tissue wet weight. Similar values were obtained for the glucose and sulfanilic acid ECS. If the interstitial space, an expression independent of the tissue blood content is used as space parameter, no significant differences were found under any of the present experimental conditions.
Animals↗
New kinetic procedure for the measurement of conjugated bilirubin with a centrifugal analyzer.
A procedure has been developed for the automated measurement of conjugated bilirubin in serum with a centrifugal analyzer. The conjugated bilirubin is measured by a fixed time kinetic method which monitors the reaction between conjugated bilirubin and diazotized sulfanilic acid at 550 nm. Results are calculated based on a comparison of the reagent blank-corrected absorbance changes between 15 seconds and 75 seconds for sample vs changes in an empirical standard. The standard used is N-(1-naphthyl) ethylene diamine dihydrochloride (NEDC) which reacts with diazotized sulfanilic acid at a rate comparable to conjugated bilirubin. The standard is calibrated by comparison with a modified Jendrassik and Grof procedure using a serum blank-corrected centrifugal analyzer reference method. The method is linear to 150 mg per 1 with a sensitivity of 3.0 milliabsorbance units per 1.0 mg per 1 of conjugated bilirubin using a 35 mul sample volume. Within-run precision is 1 percent for elevated concentrations of bilirubin. Hemolysis introduces a negative interference, the nature of which is discussed.
Bilirubin↗
Mg2+-ATPase as a membrane ecto-enzyme of human granulocytes. Inhibitors, activators and response to phagocytosis.
(1) The Mg2+-ATPase of purified human granulocytes is located at the plasma membrane. Thus, no additional enzyme activity was detected when the cells were disrupted. Moreover, the Mg2+-ATPase activity of intact cells was inhibited by such poorly permeant reagents as diazotized sulfanilic acid and suramin. Finally, the enzyme activity of cell homogenates was recovered in particulate fractions. (2)The surface Mg2+-ATPase of human granulocytes had an apparent Km of 50 microns for ATP and displayed substrate inhibition. (3) The enzyme was not affected by ouabain, but was inhibited by N-ethyl malemide, sodium meta-periodate, suramin and diazotized sulfanilic acid. The enzyme was activated by cytochalasins B and D and by UDP. Activation by UDP was characterized by changes in the enzyme's apparent Km and V and by belief of substrate inhibition. (4)Internalization of surface membranes subsequent to phagocytosis of suitable particles did not result in depletion of Mg2+-ATPase from the cell surface. The enzyme activity did not decrease after exposure to several varieties of paraffin oil emulsion particles, even if the challenged cells had been pretreated with colchicine of cytochalasin B. (5) Since suramin, which inhibited Mg2+-ATPase, had no effect upon other granulocyte functions such as chemotaxis, superoxide anion generation, or phagocytosis, it is unlikely that the enzyme plays a major role in these functions.
Adenosine Triphosphatases↗
Improved colorimetric method for determining nitrate and nitrate in foods.
A method is described for determining nitrate and nitrite in cured meat products, cheeses, and vegetables. The nitrite is determined colorimetrically by diazotization of sulfanilic acid and subsequent coupling with N-(1-naphthyl)-ethylenediamine. The concentration of nitrate plus nitrite is determined similarly but after reduction of the nitrate to nitrite on a cadmium column. The difference of the 2 values is a measure of the nitrate concentration. The main improvements are replacing the Griess reagent, which contains a carcinogen, with a mixture of sulfanile acid and N-(1-naphthyl)-ethylenediamine, providing for adjustment of pH of the sample suspension during extraction and digestion by heating, and maintaining constant pH by controlled addition of buffers and acids during color development. The method was successfully applied to the analysis of 15 samples of meat products, 23 cheeses, and 6 different vegetables. The average recovery of sodium nitrite added at levels ranging from 10 to 30 ppm was 95% and recovery of sodium nitrate added at levels from 30 to 400 ppm was 94% (corrected for cadmium column efficiency).
Animals↗
Colorimetric assay for guaiacol O-methyltransferase.
A relatively simple colorimetric assay was developed for guaiacol O-methyltransferase. Monomethylated phenolic acid substrates are enzymatically methylated to their corresponding dimethoxyl compounds; S-adenosylmethionine serves as the methyl donor. Enzymatic activity is measured by colorimetric assay of the monomethylated (nonreacted) substrate by coupling of the phenolic acid with a diazotized sulfanilic acid. The methoxyl and hydroxyl groups may be in the 3,4- or 4,3-positions on the substrate molecules; however, a side chain (COOH) or a substituted side chain is necessary for enzyme action. The radioactive demonstration of guaiacol O-methyltransferase as a separate entity from catechol O-methyl-transferase was confirmed.
Colorimetry↗
Tartrazine and the prostaglandin system.
The effect of tartrazine on prostaglandin production was evaluated in several in vitro systems in order to elucidate the interrelationship between aspirin-sensitive asthma and tartrazine. Unlike the nonsteroidal anti-inflammatory drugs, tartrazine did not inhibit cyclooxygenase activity in sheep seminal vesicles, guinea pig lung microsomes, and human platelets. Tartrazine had no effect on the activation of acyl hydrolase, which is the rate-limiting step in prostaglandin production. The major metabolite of tartrazine, sulfanilic acid, also had no inhibitory effect on the sheep seminal vesicle cyclooxygenase. In view of these findings, if there is a cross-sensitivity between tartrazine and aspirin in aspirin-sensitive asthmatics, it is unlikely to be on the basis of prostaglandin inhibition.
Animals↗
Cross immunological reactions between three haptens of the "para" group and 4-aminoantipyrine.
Cross passive hemagglutination reactions between sulfanilic acid (SA), para-aminobenzoic acid (PABA), p-phenethidine (PT) and 4-aminoantipyrine (4-AA) haptens have been investigated using conjugates of diazo derivaties of these compounds with homologous serum proteins. Intense cross passive hemagglutination reactions were found between PABA, SA and 4-AA haptens. Although anti-PT sera cross reacted intensely with PABA, SA as well as with 4-AA haptens, antibodies cross reacting with PT were not detected in any of the anti-PABA, anti-SA and anti-4-AA antisera. The conjugates containing a heterologous hapten de not substantially alter the titer of the hemagglutination reactions performed with erythrocytes coated with the homologous hapten, but completely suppress the hemagglutination reactions performed with erythrocytes coated with this hapten as well as with other, but not all, heterologous, haptens. The results support the conclusion that the apparent polysensitization to drugs may actually rely upon cross reactions with haptens chemically related to the immunizing one.
4-Aminobenzoic Acid↗
Increased responsiveness to macrophage-activating factor (MAF) after alteration of macrophage membranes.
Guinea pig macrophages pretreated with the esterase inhibitor, antithrombin III (AT III) show increased responsiveness to macrophage-activating factor (MAF) as demonstrated by their enhanced cytotoxicity for tumor cells. Other proteins that are not esterase inhibitors did not enhance the effect of MAF on the macrophage. Enhancement of MAF activity was also obtained when macrophages were preincubated with the cell surface reactant, diazotized sulfanilic acid (DSA). These studies indicate that the effect of MAF can be enhanced by chemical modifications of the macrophage membrane. They also provide further evidence to support the hypothesis that an esterase on the macrophage membrane modulates this cell's responsiveness to lymphocyte mediators.
Animals↗
Diazoniobenzenesulfonate as marker for cell surface proteins: study of the surface coat of Trypanosoma congolense.
It is possible to label selectively the surface coat of Trypanosoma congolense with radioactive sulfanilic acid diazonium salt. As demonstrated by both sodium dodecylsulfate polyacrylamide gel electrophoresis and isoelectric focusing, radioactivity is incorporated into only one protein, which has a molecular weight of 57 000 and an isoelectric point of 6.25. This indicates that the surface coat of T. congolense is a homogeneous layer, composed of molecules of one type of protein.
Animals↗