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PubMedDate not supplied

Evaluation of some arylhydrazones of p-aminobenzoic acid hydrazide as antimicrobial agents and their in vitro hepatic microsomal metabolism.

Benzoic acid p-amino-[(substituted phenyl/pyridyl) methylene] hydrazide derivatives were synthesised by interaction of p-aminobenzoic acid hydrazide with various aromatic aldehydes. The structures of the compounds were elucidated by use of their UV, IR, 1H-NMR and mass spectral data. These compounds were also evaluated for antimicrobial activity. The in vitro hepatic microsomal metabolism of benzoic acid p-amino-[(4-fluorophenyl)methylene]hydrazide (2d), a selected prototype from these compounds was also carried out.

Animals↗
PubMed2004

Phosphorescence properties of p-aminobenzoic acid immobilized on a nylon membrane.

The properties of nylon as a new material for obtaining room-temperature phosphorescence from p-aminobenzoic acid (PABA) have been investigated. Although PABA shows native phosphorescence when adsorbed on a nylon membrane, a significant improvement in both sensitivity and limit of detection is achieved in the presence of alpha-cyclodextrin and heavy atoms. An additional enhancement of the phosphorescence signal is attained when the measurements are carried out under a nitrogen atmosphere. The analytical figures of merit obtained under the best experimental conditions are: linear calibration range from 0.6 to 6 ng/spot (the lowest value corresponds to the quantitation limit); correlation coefficient, 0.998 for 18 data points; relative standard deviation, 2.2% (n = 5) at a level of 2.4 ng/spot; and limit of detection, 0.2 ng/spot (calculated according to Clayton's definition).

Journal Article↗
PubMed2005

Halogeno-substituted 2-aminobenzoic acid derivatives for negative ion fragmentation studies of N-linked carbohydrates.

Negative ion electrospray mass spectra of high-mannose N-linked glycans derivatised with 2-aminobenzoic acids and ionised from solutions containing ammonium hydroxide gave prominent [M-H](-) ions accompanied by weaker [M-2H](2-) ions. Fragmentation of both types of ions gave prominent singly charged glycosidic cleavage ions containing the derivatised reducing terminus and ions from the non-reducing terminus that appeared to be products of cross-ring cleavages. Differentiation of these two groups of ions was conveniently achieved in a single spectrum by use of chloro- or bromo-substituted benzoic acids in order to label ions containing the derivative with an atom with a distinctive isotope pattern. Fragmentation of the doubly charged ions gave more abundant fragments, both singly and doubly charged, than did fragmentation of the singly charged ions, but information of chain branching was masked by the appearance of prominent ions produced by internal cleavages.

Halogens↗
PubMed1997

C-cytosolic and transmembrane domains of the N-benzoyl-L-tyrosyl-p-aminobenzoic acid hydrolase alpha subunit (human meprin alpha) are essential for its retention in the endoplasmic reticulum and C-terminal processing.

N-benzoyl-L-tyrosyl-p-aminobenzoic acid hydrolase (PPH, human meprin) is a member of the astacin family of Zn-metalloendopeptidases and is highly expressed in the microvillus membrane of human small intestinal epithelial cells. It is a type I transmembrane protein consisting of differentially processed glycosylated alpha and beta subunits. Biosynthesis experiments using transfected, metabolically labelled simian virus 40 (SV40) transformed african green monkey kidney cells (COS-1) and Madin Darby canine kidney (MDCK) cells, have previously shown that PPH alpha was retained in the endoplasmic reticulum (ER) and that for subsequent secretion removal of the alpha-tail was necessary [Grünberg, J., Dumermuth, E., Eldering, J. A. & Sterchi, E. E. (1993) FEBS Lett. 335, 376-379]. We proposed an involvement of the alpha-tail in ER retention. To investigate the possible role of the transmembrane and/or the C-terminal domain of the alpha-subunit, tailswitch mutants were constructed in which these domains were exchanged between the alpha and beta subunits. Biosynthesis and post-translational processing of these mutants were investigated in transiently transfected COS-1 cells. The beta/alpha tailswitch mutant, in which the transmembrane and C-cytosolic parts of PPH beta were substituted by the corresponding parts of the PPH alpha subunit, was transported much slower compared with the wild-type PPH beta subunit. In addition, fusion of the alpha-tail to a C-terminally truncated secretory form of PPH alpha leads to its retention in the ER. This mutant, but not the secretory form, coimmunoprecipitated with calnexin, indicating an involvement of this molecular chaperone in retaining PPH alpha in the ER. The alpha/beta tailswitch mutant, in which the transmembrane domain and the C-cytosolic part of PPH alpha were substituted by the corresponding parts of PPH beta, was processed less efficiently in comparison with PPH alpha, resulting in a lower secretion rate. Taken together these data suggest a role of the alpha-tail in mediating association with ER-resident machinery, facilitating C-terminal processing.

Animals↗