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p-Aminobenzoic acid (PABA) exerts three metabolic effects on E. coli: it acts as a normal vitamin at low concentrations, as a source of another vitamin, p-hydroxybenzoic acid (POB), at moderate concentrations, and as a growth inhibitor at high concentrations (150 to 1600 microg./ml.). The inhibition is competitively reversed by POB in 1/100 the concentration of PABA. The inhibition is also reversed to a limited extent by shikimic acid and compound X, precursors of POB. p-Nitrobenzoic acid is an inhibitory competitor of both POB and PABA. The retardation of growth produced by PABA and other competitive analogues of POB (p-nitrobenzoic acid; 4,4'-dihydroxydiphenyl sulfone; phenosulfazole) is converted to complete bacteriostasis by the addition of L-aspartic acid in a remarkably low concentration (1 microg./ml.)) without change in the competitive ratio with POB. The mechanism underlying this synergism is not clear. In contrast to wild type, mutants that require POB not only are inhibited by much lower concentrations of the above analogues, but also show inhibition by weaker competitors of POB such as p-hydroxybenzenesulfonamide, p-chlorobenzoic acid, and p-fluorobenzoic acid.
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p-Aminobenzoic acid (PABA) is a cyclic amino acid, belongs to the vitamin B group, and is used as a protective drug against solar insolation and in diagnostic tests for the state of the gastrointestinal tract in medicine. We were the first to establish that PABA is an inducer of endogenous interferon and immunomodulator and displays a virucidal, synergistic antiviral effect when combined with chemical drugs and the properties of a direct anticoagulant. Based on these properties, we elaborated a new medicinal drug "Actipol" which was introduced in clinical practice.
O-aminobenzoic acid (o-ABA) film is deposited on glassy carbon electrode (GCE) by electropolymerization in pH 7.0 phosphate buffer solution (PBS). The polymeric film shows an excellent electrocatalytical activity on the oxidation of dopamine (DA). Difference pulse voltammetry (DPV) was performed to determine DA in an excess of ascorbic acid (AA). The oxidation peak potentials of DA and AA recorded are 144 mV and -52 mV, respectively. In pH 7.0 PBS, the anodic peak current of DA increases linearly over two concentration intervals, viz., 1.0x10(-7)-1.0x10(-5) mol L(-1) and 1.0x10(-5) - 2.0x10(-4) mol L(-1), with correlation coefficient, 0.9966 and 0.9960, respectively. The relative standard deviation of 10 successive scans is 2.8 % for 1.0x10(-6) mol L(-1) DA and the recovery is 96 % - 101 %. The interference of AA and DOPAC with the determination of DA could be eliminated because of the very distinct attracting interaction between DA cations and the negatively poly (o-ABA) film in pH 7.0 PBS. The proposed method exhibits good recovery and reproducibility.
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The antibacterial activity of p-aminobenzoic acid against Listeria monocytogenes, Salmonella enteritidis and Escherichia coli was compared with the activity of commonly used acidulants: formic, propionic, acetic, lactic and citric acids. Viable count evaluations and MIC determinations indicated that p-aminobenzoic acid caused greater inhibitory effects than the other organic acids. The activity of p-aminobenzoic acid on the growth of the test organisms at selected pH values indicated that p-aminobenzoic acid was more active at low pH than at high pH. Uptake studies showed that the uptake of p-aminobenzoic acid by E. coli was markedly decreased as the pH values increased. Electron micrographs of E. coli cells grown in the presence of p-aminobenzoic acid indicate that p-aminobenzoic acid caused marked damage to the cell envelope. It is suggested that p-aminobenzoic acid has at least two mechanisms of action: one mechanism in common with other organic acids and the other mechanism by interfering with the synthesis of the peptidoglycan layer by an action on the dihydrofolate reductase enzyme.
We have previously reported that human lymphoid cells, such as peripheral blood mononuclear leukocytes (PBML) and the T-cell leukemia line Jurcat, synthesize p-acetamidobenzoic acid from p-aminobenzoic acid (PABA) and a two carbon fragment from arachidonic acid (AA), conceivably derived from beta-oxidation. Here we demonstrate that AA is a preferred substrate in this acetylation reaction over other common fatty acids such as palmitic (PA), oleic, linoleic or linolenic. This was unexpected because AA is not considered as a fuel fatty acid. In Jurcat cells, AA is also preferred as a substrate for beta-oxidation over PA. In contrast, in PBML, PA was clearly preferred as substrate for beta-oxidation over AA, in accordance with previous observations. The difference between Jurcat cells and PBML was not dependent on culture conditions, because phytohemagglutinin and interleukin-2 activated PBML, kept in culture, showed the same PA preference as freshly prepared non-activated PBML. Furthermore, we observed differences between Jurcat cells and PBML in their relative content of fatty acids and in the incorporation of PA and AA into triacylglycerols and phospholipids. Taken together, our results show differences in beta-oxidation between Jurcat cells and PBML, and suggest the involvement of peroxisomal, besides mitochondrial, beta-oxidation, in the acetylation of PABA with fatty acids as acetyl donors.
A new, selective, and sensitive ion-pair RP-HPLC method for the simultaneous determination of three classes of natural organic compounds, i.e., carbohydrates, amino sugars, and uronic acids, in environmental samples is presented. p-Aminobenzoic acid is used for precolumn derivatization of the analytes, enabling fluorescence (lambda(ex) 313 nm, lambda(em) 358 nm) or photometric detection (303 nm). The dependence of the derivatization yield on the reaction conditions is examined. Derivatives of lactose, galactose, glucose, mannose, xylose, arabinose, galacturonic acid, glucuronic acid, N-acetylglucosamine, and glycerinealdehyde were separated on a RP-C18 column with hydrophilic end capping within 35 min, applying TBAHSO4 as the ion-pair reagent. The concentration detection limits range between 20 and 30 microg L(-1) ((1-2) x 10(-7) M) for fluorescence detection and between 30 and 75 microg L(-1) for UV detection. A good linearity is achieved in the concentration range from 50 microg L(-1) to 100 mg L(-1) (r2 > 0.99). The described method has been applied for the determination of mono-/disaccharides, uronic acids, and amino sugars in soil solutions and in landfill leachates.
OBJECTIVE: This study investigated the biosynthesis of P-aminobenzoic acid by Streptococcus sanguis and the role of P-aminobenzoic acid in the interaction between Streptococcus sanguis and Streptococcus mutans. METHODS: A reversed-phase high-performance liquid chromatographic technique was used to analyze the P-aminobenzoic acid synthesized by Streptococcus sanguis in an anaerobic atmosphere. RESULTS: The results showed, that (1) the chromatographic method established in this study had good linear relation and the average recovery of P-aminobenzoic acid was 80%, and (2) Streptococcus sanguis did synthesize P-aminobenzoic acid, and the mean concentration of P-aminobenzoic acid was 1.23 micrograms/mL. CONCLUSIONS: The results of this study will help further studies of the factors that may have effects on P-aminobenzoic acid synthesis by Streptococcus sanguis and on the role of P-aminobenzoic acid in the microbial homeostasis of dental plaque.
The molecular complex lumiflavin-2-aminobenzoic acid monohydrate (C13H12N4O2.C7H7NO2.H2O) crystallizes from from aqueous solution as red triclinic prisms. The space group is P1 with cell dimensions a = 9.660 A, b = 14.866 A, c = 7.045 A, alpha = 95.44 degrees , beta = 95.86 degrees, and gamma = 105.66 degrees . The crystal structure was solved by direct methods and refined by block-diagonal least-squares procedures to an R value of 0.050 on the basis of 1338 observed reflections. The structure is composed of stacks of alternating lumiflavin adn un-ionized (neutral) 2-aminobenzoic acid molecules. Two different modes of stacking interaction are observed. In one, 2-aminobenzoic acid overlaps all three of the isoalloxazine rings, at a mean distance of 3.36 A; in the other, 2-aminobenzoic acid interacts distance of 3.36 A; in the other, 2-aminobenzoic acid interacts with the pyrazine and dimethylbenzene moieties, at a distance of 3.42 A. Perpendicular to the stacking direction, the molecules form a continuous sheet. Each flavin is hydrogen bonded via O(2) and NH(3) to two symmetrically related aminobenzoates; the water of crystallization forms three hydrogen bonds, bridging two flavins, via O(4) and N(5), and one aminobenzoic acid. The red color of the crystals results from a charge-transfer transition involving stacked flavin and 2-aminobenzoic acid. The red color of the crystals results from a charge-transfer transition involving stacked flavin and 2-aminobenzoic acid molecules. Measurements of the polarized optical absorption spectra of crystals show that the transition moment direction for the long wavelength absorbance (beyond 530 nm) contains an out-of-plane component which can only arise from a charge-transfer interaction. Since the amino N does not make exceptionally close interactions with isoalloxazine atoms in either stacking mode (minimum interatomic distance 3.52 A), the charge transfer is presumed to involve pi orbitals of the 2-aminobenzoic acid donor.
Intestinal uptake of p-aminobenzoic acid was examined by means of an in vitro everted sac technique in rats immunized with ovalbumin-p-aminobenzoic acid conjugate. A dose-dependent and antigen-specific decrease in the serosal transfer of p-aminobenzoic acid was observed in rats immunized 6 times with protein-hapten conjugate compared with the control. There was a significant increase in the recovery of p-acetamidobenzoic acid, a metabolite of p-aminobenzoic acid, in mucosal fluid, tissue, and serosal fluid in the jejunum. In the case of ileum, increase of p-acetamidobenzoic acid was observed in mucosal fluid. However, there was no significant effect in the ileal p-acetamidobenzoic acid in tissue and serosal fluid between immunized and non-immunized rats. To examine the increased metabolism of immunized rats, N-acetyltransferase activity of the small intestinal mucosa was examined. There was a significant increase in mucosal N-acetyltransferase activity in immunized rats compared with the control animals. These observations suggested that the mucosal immune system may play an important role in regulating the intestinal uptake of the low molecular weight compounds.
Syntheses of amino acid derivatives of p-aminobenzoic acid and 2,6-xylidine, potential antiarrhythmic agents are described. The carbodiimide method and the method of mixed anhydrides were employed for the syntheses. Physicochemical properties, yields, data of elementary analysis, and IR and 1H-NMR spectra of eighteen novel compounds are given.
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