Disease relevance of Shinnippon Fast Red GG Base

• In a new method of testing stool samples from newborn babies for cystic fibrosis (C.F.), a colourless substrate, benzoyl-arginine-p-nitroanilide (B.A.P.N.A.), releases yellow p-nitroaniline when hydrolysed by trypsin [1].
• Coupling of diazotized p-nitroaniline to catecholamines and their metabolites in urine has been proposed for use in screening for secreting neuroblastoma in childhood [2].
• Only strains of Bacillus cereus were able to acetylate 4-nitroaniline and 3,5-dimethyl-4-nitroaniline [3].
• Here we demonstrate that MEKC differentiates between the enzymatic activities of Pseudomonas aeruginosa elastase (PsE) and human leukocyte elastase (HLE) or cathepsin G (Cat G) in assays using the chromogenic peptide substrates Suc-Ala-Ala-Ala-NA or Suc-Ala-Ala-Pro-Phe-NA, respectively (where Suc = succinyl and NA = 4-nitroaniline/u-nitroanilide) [4].
• Except for 4-nitroaniline (the only chemical in the examined group that required activation to become the Michael receptor), all chemicals containing reactive substructures revealed excess toxicity over polar narcosis QSAR for E. coli endpoints [5].

High impact information on Shinnippon Fast Red GG Base

• This medium did not cause cleavage of p-nitroaniline from the tripeptide substrate, and 83% of added FVIII procoagulant activity remained after 48 hr [6].
• When the synthetic tripeptide was incubated in contact with cultured endothelial cells, 7.3 +/- 0.8 X 10(-10) moles of p-nitroaniline/hr was released; moreover, only 47% of the added FVIII procoagulant activity remained after 48 hr [6].
• The AMC and pNA groups give insights into the leaving group binding site (P') of cathepsin B. These studies show for the first time that at least seven dissociable groups are involved in substrate binding and hydrolysis in cathepsin B activity [7].
• Analysis of the observed molar transition energies indicates that for 4-nitroaniline and N,N-dimethyl-4-nitroaniline the stabilization of the zwitterionic excited states of such push-pull molecules is on the order of 2.0 kcal mol(-1) per mol of added salt [8].
• A new solid ionic crystal MALDI matrix was synthesized which combined the lipid response enhancing UV-absorber p-nitroaniline with the protonating agent butyric acid [9].

Chemical compound and disease context of Shinnippon Fast Red GG Base

• Subchronic inhalation toxicity of p-nitroaniline and p-nitrochlorobenzene in rats [10].

Biological context of Shinnippon Fast Red GG Base

• Protease activity was quantitated by the hydrolysis of p-nitroaniline from the substrate, N-benzoyl-phenylalanyl-valyl-arginyl-p-nitroanilide and by degradation of the procoagulant activity of added purified plasma FVIII/vWF protein [6].
• A comparative assessment of reductive amination and cleavage of these linkers under conditions of multiple synthesis indicated that both were applicable to a broad range of primary amines including aniline and 4-nitroaniline [11].
• The three diaminobenzenes and 4-nitroaniline were mutagenic only with metabolic activation [12].
• It is rate-determining with the ester substrate, but with the 4-nitroaniline acylation is and this is even more pronounced with the amide [13].
• A novel method to characterize the activity and reaction kinetics of the immobilized enzyme has been developed based on the frontal analysis of enzymatic reaction products, which was performed by the on-line monitoring of the absorption at 410 nm of p-nitroaniline from the hydrolysis of N-alpha-benzoyl-DL-arginine-p-nitroanilide (BAPNA) [14].

Anatomical context of Shinnippon Fast Red GG Base

• To address these limitations, a series of 4-nitroaniline mustards bearing hydrophilic side chains attached via an electron-withdrawing carboxamide group was prepared and evaluated for hypoxia-selective cytotoxicity against Chinese hamster cell lines [15].
• Metabolism of 4-nitroaniline by rat liver microsomes [16].
• The localization of gamma-glutamyl transferase (GGT) in the intact rat liver was studied by a new approach in which the chromogenic gamma-glutamyl donor substrate of GGT gamma-glutamyl-p-nitroanilide is perfused through the portal vein to yield p-nitroaniline, which is monitored spectrophotometrically [17].
• Infusion of glutathione (GSH), the natural substrate of GGT, was shown to markedly reduce or to abolish the formation of p-nitroaniline without entering the liver cells, indicating the existence of a GGT ectoactivity accessible to the sinusoidal circulation [17].
• An enzymatic activity with releases p-nitroaniline from 3-carboxypropionyl-trialanine p-nitroanilide (Suc[Ala]3NA) was characterized in blood plasma of patients with Tangier disease [18].

Associations of Shinnippon Fast Red GG Base with other chemical compounds

• A 5-min irradiation of S. cerevisiae with 2.4 microM Leu-p-NA or 15 microM Leu-Leu-Phe(4N3,2NO2) causes 50% inhibition of trimethionine uptake. p-Nitroaniline, a possible hydrolysis product generated from Leu-p-NA by cellular peptidase activity, has no effect on peptide transport [19].
• The PNA is then diazotized with sodium nitrite and subsequently coupled to a chromogen, N-(1-naphthyl)-ethylenediamine dihydrochloride (NED) to produce a deep pink/magenta colored azo-dye at the site of oxytocinase activity [20].
• The purified enzyme catalyzed hydrolysis and transpeptidation of various gamma-glutamyl compounds, including the oxidized and reduced forms of glutathione, gamma-glutamyl compounds of L-phenylalanine, L-tyrosine, L-histidine, L-alpha-aminobutyrate, L-leucine, and p-nitroaniline [21].
• Liquid glycerol/carbohydrate mixtures could be used directly to record MALDI spectra on the soft-landed compounds provided they were fortified in advance with traditional MALDI matrices such as p-nitroaniline and alpha-cyano-4-hydroxycinnamic acid [22].
• Computer simulation of the linear and nonlinear optical susceptibilities of p-nitroaniline in cyclohexane, 1,4-dioxane, and tetrahydrofuran in quadrupolar approximation. I. Molecular polarizabilities and hyperpolarizabilities [23].

Gene context of Shinnippon Fast Red GG Base

• Kallikrein-like activity was expressed as picomoles of p-nitroaniline liberated per minute per milligram of protein [24].
• In the standard method, we defined the activity of h-TM forming 0.1 micromol of p -nitroaniline per min in the reaction as 1 JRS Unit [25].
• Due to the low equilibrium population of the X-cis-Pro-Phe-pNA isomer (the PPIase substrate), in conjunction with the low solubility of p-nitroaniline generated by chymotrypsin hydrolysis, substrate concentrations in the saturating region are not experimentally attainable [26].
• Conditions were chosen such that the rate of para-nitroaniline release from the substrate is directly proportional to the concentration of tPA [27].
• The scu-PA solution was activated by plasmin to two-chain u-PA, which releases p-nitroaniline from pyro-Glu-Gly-Arg-pNA, and the optical density at 405 nm was measured [28].

Analytical, diagnostic and therapeutic context of Shinnippon Fast Red GG Base

• Sensitive determination of carbohydrates labelled with p-nitroaniline by capillary electrophoresis with photometric detection using a 406 nm light-emitting diode [29].
• We have coupled diazotized p-nitroaniline to catecholamines, derivatives, and metabolites and examined the reaction products by thin-layer chromatography and physico-chemical methods (ultraviolet spectra, mass spectroscopy, nuclear magnetic resonance) [2].
• The release of p-nitroaniline was more prolonged, but still showed little dependence on microsphere size [30].
• Glycosylamination was performed with p-nitroaniline in DMSO-formic acid-water, where the whole mixture of oligosaccharide derivatives was isolated by reversed phase HPLC on Hamilton PRP-1 and separated into single glycosylamines on Shandon Hypersil ODS [31].
• 4. Given the relatively high frequency of organic acidurias, particularly methylmalonic aciduria, in intensive care unit populations, it is suggested that the p-nitroaniline reaction be incorporated into the battery of chemical urine tests [32].

References