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At least 397 records · Page 22Linked to original sources
PubMed1978

Characterization of p-aminobenzoic acid transport across the rat intestine.

The intestinal absorption of PABA, a member of the vitamin B complex, was characterized in vivo and in vitro in the rat by the segmental intestinal perfusion and everted gut sac technique. Net PABA absorption was directly proportional to substrate concentration, and saturation of absorption did not occur with increasing concentrations of PABA (1 to 50 mM), indicating a nonsaturable process. Jejunal and ileal absorption rates were similar and were not influenced by the presence of glucose or the absence of sodium in the test solution. Similarly, 14C-PABA transport in vitro was nonsaturable and proportional to PABA concentration (0.05, 0.5, 1, 10, and 50 mM). It was not inhibited by ouabain or other PABA analogues such as folic acid and benzoic acid. These studies indicate that PABA, a vitamin B cofactor, is absorbed by a nonsaturable, sodium-independent process, which characterizes passive diffusion and is similar to the absorption of other vitamin B members.

4-Aminobenzoic Acid↗
PubMed1997

Mechanism of inactivation of myeloperoxidase by 4-aminobenzoic acid hydrazide.

Hypochlorous acid is the most powerful oxidant generated by neutrophils and is likely to contribute to the damage mediated by these inflammatory cells. The haem enzyme myeloperoxidase catalyses its production from hydrogen peroxide and chloride. 4-Aminobenzoic acid hydrazide (ABAH) is a potent inhibitor of hypochlorous acid production. In this investigation we show that, in the presence of hydrogen peroxide, ABAH irreversibly inactivates myeloperoxidase. ABAH was oxidized by myeloperoxidase, and kinetic analysis of the inactivation conformed to that for a mechanism-based inhibitor. Inactivation was exacerbated by concentrations of hydrogen peroxide greater than 50 microM and by the absence of oxygen. Hydrogen peroxide alone caused minimal inactivation. Reduced glutathione inhibited the oxidation of ABAH as well as the irreversible inhibition of myeloperoxidase. In the presence of oxygen, ABAH and hydrogen peroxide initially converted myeloperoxidase into compound III, which subsequently lost haem absorbance. In the absence of oxygen, the enzyme was converted into ferrous myeloperoxidase and its haem groups were rapidly destroyed. We propose that myeloperoxidase oxidizes ABAH to a radical that reduces the enzyme to its ferrous intermediate. Ferrous myeloperoxidase reacts either with oxygen to allow enzyme turnover, or with hydrogen peroxide to give irreversible inactivation.

Aniline Compounds↗
PubMed1989

[Amino acid derivatives of 2,6-xylidine and p-aminobenzoic acid. II. Synthesis of derivatives of N-(p-aminobenzoylaminoalkylacyl)-2,6-xylidines and study of their resistance to proteolytic factors].

Syntheses of N-(p-aminobenzoylaminoalkylacyl)-2,6-xylidines 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 spectra of eighteen novel compounds are given. Resistance of some obtained compounds to actions of the gastric digestive juice and the intestinal one was tested.

Aniline Compounds↗
PubMed2000

The use of the 2-aminobenzoic acid tag for oligosaccharide gel electrophoresis.

Gel electrophoresis of fluorophore labeled saccharides provides a rapid and reliable method to screen enzymatic and/or chemical treatments of polysaccharides and glycoconjugates, as well as a sensitive and efficient microscale method to separate and purify oligosaccharides for further analysis. A simple and inexpensive method of derivatization and analysis using 2-aminobenzoic acid (anthranilic acid, AA) is described and applied to the extracellular polysaccharide released by the desiccation tolerant cyanobacterium Nostoc commune DRH-1. The results of these analyses suggest a possible protective functionality of two pendent groups, as well as a potential relationship between these groups and the desiccation tolerance of the organism.

Carbohydrate Sequence↗
PubMed1999

3-Aminobenzamide and 3-aminobenzoic acid, tags for capillary electrophoresis of complex carbohydrates with laser-induced fluorescent detection.

The efficiencies in derivatization of reducing carbohydrates were compared by capillary electrophoresis using maltose as a model with nine monoaminobenzene derivatives by reductive amination in the presence of sodium cyanoborohydride. We found that aminobenzene derivatives substituted at the 3-position showed good reactivity with reducing carbohydrates as expected from the reaction mechanism, although the fluorescence intensities and molar absorptivities of these derivatives were not as high as those of 2- and 4-aminobenzene derivatives. The reagents, 3-aminobenzamide and 3-aminobenzoic acid, which showed the highest reactivity, were applied to the labeling of carbohydrate chains obtained from some sialic acid-containing glycoprotein samples, and also high-mannose and hybrid-type oligosaccharides. Capillary electrophoresis of these labeled carbohydrate chains in an inner surface-modified capillary with (50% phenyl)methylpolysiloxane allowed excellent separation of sialic acid-containing carbohydrate chains derived from fetuin and thyroglobulin as well as high mannose-type and hybrid-type carbohydrates derived from bovine pancreas ribonuclease B, soybean agglutinin and hen ovalbumin. The lower limit of calibration was as low as the 10(-16) mol (injected amount) with helium-cadmium laser induced detection.

Aminobenzoates↗
PubMed1987

Optimal concentration of p-aminobenzoic acid and folic acid in the in vitro assay of antifolates against Plasmodium falciparum.

In vitro tests for Plasmodium falciparum sensitivity to pyrimethamine, sulfadoxine, and both drugs in combination were performed in four kinds of culture medium, each differing in p-amino benzoic acid (PABA) and folic acid concentrations. Results of the tests using pyrimethamine-sensitive and pyrimethamine-resistant isolates indicated that drug activity was reduced proportionally to the concentrations of these two growth factors in the medium. The optimal concentrations of PABA and folic acid for parasite growth and drug susceptibility, as evaluated by microscopic examination and by the extent of incorporation of radioactive 14C-pyrimethamine and 14C-sulfadoxine, were 10 ng/ml and 2 ng/ml, respectively. Depletion of PABA and folic acid from the medium had no effect on drug-resistant parasites but multiplication of drug-sensitive isolates was markedly reduced. Medium containing 0.5 ng/ml PABA and 10 ng/ml folic acid was the best for parasite growth regardless of the degree of drug sensitivity. Results obtained by using this medium agreed most closely with results from in vivo observations.

4-Aminobenzoic Acid↗