scholarly journals CONFIRMATORY EVIDENCE OF THE CHROMOTRICHIAL ACTIVITY OF p-AMINOBENZOIC ACID

1941 ◽  
Vol 138 (1) ◽  
pp. 441
Author(s):  
Gustav J. Martin ◽  
S. Ansbacher
Keyword(s):  
Aminobenzoic Acid

Simultaneous Spectrophotometric Determination of Salbutamol by Coupling with Diazotized 4-Aminobenzoic acid

2017 ◽  
Vol 8 (1) ◽  
Author(s):  
Hind Hadi ◽  
Gufran Salim
Keyword(s):  
Pharmaceutical Preparations ◽  
Coupling Reaction ◽  
Dosage Forms ◽  
Water Soluble ◽  
Trace Determination ◽  
Aminobenzoic Acid ◽  
Optimum Conditions ◽  
Colored Product ◽  
Versus Concentration

A simple, rapid and sensitive spectrophotmetric method for trace determination of salbutamol (SAL) in aqueous solution and in pharmaceutical preparations is described. The method is based on the diazotization coupling reaction of the intended compound with 4-amino benzoic acid (ABA) in alkaline medium to form an intense orange, water soluble dye that is stable and shows maximum absorption at 410 nm. A graph of absorbance versus concentration indicates that Beer’s law is obeyed over the concentration range of 0.5-30 ppm, with a molar absorbtivity 3.76×104 L.mol-1 .cm-1 depending on the concentration of SAL. The optimum conditions and stability of the colored product have been investigated and the method was applied successfully to the determination of SAL in dosage forms.

Relationship between ambient temperature and acetylating capacity of human blood

1963 ◽  
Vol 18 (5) ◽  
pp. 955-958 ◽  
Author(s):  
S. H. Blondheim ◽  
Gabriel Neumann ◽  
Edna Kott ◽  
Zena Ben-Ishai
Keyword(s):  
Ambient Temperature ◽  
Human Blood ◽  
Aromatic Amines ◽  
September 11 ◽  
Aminobenzoic Acid ◽  
Heat Acclimatization ◽  
The Subject

The ability of human blood to acetylate p-aminobenzoic acid, determined in vitro, varied directly with the ambient temperature to which the subject was exposed before the blood was drawn. This was demonstrated by 135 determinations of the acetylating ability of the blood of 49 subjects performed over a period of 3 years, and also in acute experiments in which subjects were exposed to 6 and 37 C for up to 2 hr. Variations in the acetylating ability of blood may reflect the activity of metabolic mechanisms involved in thermal homeostasis. aromatic amines; p-aminobenzoic acid; cold; heat acclimatization; (blood) enzymes; weather; environment Submitted on September 11, 1962

scholarly journals Metabolites of p-Aminobenzoic Acid

1961 ◽  
Vol 236 (2) ◽  
pp. 448-454
Author(s):  
N.H. Sloane
Keyword(s):  
Aminobenzoic Acid

scholarly journals Effect of 3-Aminobenzoic Acid Ethyl Ester Methanesulfonate (MS-222) on Quality of Marine Cultured Turbot (Scophthalmus maximus) during Simulated Transport in Water

Fishes ◽  
2021 ◽  
Vol 6 (2) ◽  
pp. 20
Author(s):  
Jie Cao ◽  
Qi Wang ◽  
Jun Mei ◽  
Jing Xie
Keyword(s):  
Dissolved Oxygen ◽  
Ethyl Ester ◽  
Acid Ethyl Ester ◽  
Scophthalmus Maximus ◽  
Ammonia Nitrogen ◽  
Control Group ◽  
Aminobenzoic Acid ◽  
Transport Stress ◽  
Turbot Scophthalmus Maximus

This study evaluated the effect of different concentrations (20, 40 and 60 mg/L) of 3-aminobenzoic acid ethyl ester methanesulfonate (MS-222) on the quality changes in turbot during simulated transport in water. The results showed that the ammonia nitrogen content in the transportation water of each sample increased significantly, and the dissolved oxygen level decreased. The dissolved oxygen content in MS-222-treated samples was higher than that of control group (CK) samples. For turbot flesh quality, simulated transport in water led to a decrease in moisture, fat and protein contents in all samples. The MS-222-treated turbot samples showed higher pH values, glycogen contents, springiness and chewiness values and lower lactic acid contents comparing with the CK samples during simulated transport in water. In addition, the fresh and bitter amino acids in the muscle of turbot increased in each treatment group compared to the non-transported fish at the end of the simulated transport. The results showed that MS-222 treatment could retard the turbot transport stress and improve the quality of turbot during simulated transport in water.

scholarly journals METHIONINE REVERSAL OF 2-CHLORO-4-AMINOBENZOIC ACID INHIBITION IN ESCHERICHIA COLI

1951 ◽  
Vol 188 (2) ◽  
pp. 753-758 ◽  
Author(s):  
C.H. Wang ◽  
Tsoo E. King ◽  
Vernon H. Cheldelin ◽  
Bert E. Christensen
Keyword(s):  
Escherichia Coli ◽  
Acid Inhibition ◽  
Aminobenzoic Acid

Macrocyclic scaffolds derived from p-aminobenzoic acid

2007 ◽  
pp. 2240 ◽  
Author(s):  
Fred Campbell ◽  
Jeffrey Plante ◽  
Christopher Carruthers ◽  
Michaele J. Hardie ◽  
Timothy J. Prior ◽  
...  
Keyword(s):  
Aminobenzoic Acid

scholarly journals Mutations of folC cause increased susceptibility to sulfamethoxazole in Mycobacterium tuberculosis

2021 ◽  
Vol 11 (1) ◽  
Author(s):  
Ruiqi Wang ◽  
Kun Li ◽  
Jifang Yu ◽  
Jiaoyu Deng ◽  
Yaokai Chen
Keyword(s):  
Mycobacterium Tuberculosis ◽  
Type Strain ◽  
Wild Type Strain ◽  
Clinical Isolates ◽  
Aminobenzoic Acid ◽  
Wild Type ◽  
Dihydropteroate Synthase ◽  
Expression Levels ◽  
Encoding Gene ◽  
Increased Susceptibility

AbstractPrevious studies showed that mutation of folC caused decreased expression of the dihydropteroate synthase encoding gene folP2 in Mycobacterium tuberculosis (M. tuberculosis). We speculated that mutation of folC in M. tuberculosis might affect the susceptibility to sulfamethoxazole (SMX). To prove this, 53 clinical isolates with folC mutations were selected and two folC mutants (I43A, I43T) were constructed based on M. tuberculosis H37Ra. The results showed that 42 of the 53 clinical isolates (79.2%) and the two lab-constructed folC mutants were more sensitive to SMX. To probe the mechanism by which folC mutations make M. tuberculosis more sensitive to SMX, folP2 was deleted in H37Ra, and expression levels of folP2 were compared between H37Ra and the two folC mutants. Although deletion of folP2 resulted in increased susceptibility to SMX, no difference in folP2 expression was observed. Furthermore, production levels of para-aminobenzoic acid (pABA) were compared between the folC mutants and the wild-type strain, and results showed that folC mutation resulted in decreased production of pABA. Taken together, we show that folC mutation leads to decreased production of pABA in M. tuberculosis and thus affects its susceptibility to SMX, which broadens our understanding of mechanisms of susceptibilities to antifolates in this bacterium.

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