nitrophenols and potassium-phosphate

A new organic nonlinear optical single crystal, L-phenylalanine-4-nitrophenol (LPAPN) belonging to the amino acid group has been successfully grown by slow evaporation technique. The lattice parameters of the grown crystal have been determined by X-ray diffraction studies. FT-IR spectrum was recorded to identify the presence of functional group and molecular structure was confirmed by NMR spectrum. Thermal strength of the grown crystal has been studied using TG-DTA analyses. The grown crystals were found to be transparent in the entire visible region. The existence of second harmonic generation signals was observed using Nd:YAG laser with fundamental wavelength of 1064 nm.

Topics: Crystallization; Differential Thermal Analysis; Fourier Analysis; Magnetic Resonance Spectroscopy; Nitrophenols; Nonlinear Dynamics; Phenylalanine; Phosphates; Potassium Compounds; Powders; Spectrophotometry, Ultraviolet; Spectroscopy, Fourier Transform Infrared; Thermogravimetry; X-Ray Diffraction

The present work reports the preparation of activated carbon fiber (ACF) from Kenaf natural fibers. Taguchi experimental design method was used to optimize the preparation of ACF using K(2)HPO(4). Optimized conditions were: carbonization at 300 degrees C, impregnation with 30%w/v K(2)HPO(4) solution and activation at 700 degrees C for 2h with the rate of achieving the activation temperature equal to 2 degrees C min(-1). The surface characteristics of the ACF prepared at optimized conditions were also studied using pore structure analysis, scanning electron microscopy (SEM) and Fourier transform infrared (FT-IR) spectroscopy. Pore structure analysis shows that micropores constitute the most of the porosity of the prepared ACF. The ability of the ACF prepared at optimized conditions to adsorb phenol and p-nitrophenol from aqueous solution was also investigated. The equilibrium data of phenol and p-nitrophenol adsorption on the prepared ACF were well fitted to the Langmuir isotherm. The maximum adsorption capacities of phenol and p-nitrophenol on the prepared ACF are 140.84 and 136.99 mg g(-1), respectively. The adsorption process follows the pseudo-first-order kinetic model.

Topics: Adsorption; Biodegradation, Environmental; Carbon; Carbon Fiber; Charcoal; Hibiscus; Kinetics; Nitrogen; Nitrophenols; Phenols; Phosphates; Potassium Compounds; Temperature; Time Factors

The kinetic properties of a microsomal gill (Na(+), K(+)) ATPase from the blue crab, Callinectes danae, acclimated to 15 per thousand salinity for 10 days, were analyzed using the substrate p-nitrophenylphosphate. The (Na(+), K(+))-ATPase hydrolyzed the substrate obeying Michaelian kinetics at a rate of V=102.9+/-4.3 U.mg(-1) with K(0.5)=1.7+/-0.1 mmol.L(-1), while stimulation by magnesium (V=93.7+/-2.3 U.mg(-1); K(0.5)=1.40+/-0.03 mmol.L(-1)) and potassium ions (V=94.9+/-3.5 U.mg(-1); K(0.5)=2.9+/-0.1 mmol.L(-1)) was cooperative. K(+)-phosphatase activity was also stimulated by ammonium ions to a rate of V=106.2+/-2.2 U. mg(-1) with K(0.5)=9.8+/-0.2 mmol.L(-1), following cooperative kinetics (n(H)=2.9). However, K(+)-phosphatase activity was not stimulated further by K(+) plus NH(4) (+) ions. Sodium ions (K(I)=22.7+/-1.7 mmol.L(-1)), and orthovanadate (K(I)=28.1+/-1.4 nmol.L(-1)) completely inhibited PNPPase activity while ouabain inhibition reached almost 75% (K(I)=142.0+/-7.1 micromol.L(-1)). Western blotting analysis revealed increased expression of the (Na(+), K(+))-ATPase alpha-subunit in crabs acclimated to 15 per thousand salinity compared to those acclimated to 33 per thousand salinity. The increase in (Na(+), K(+))-ATPase activity in C. danae gill tissue in response to low-salinity acclimation apparently derives from the increased expression of the (Na(+), K( (+) ))-ATPase alpha-subunit; phosphate-hydrolyzing enzymes other than (Na(+), K(+))-ATPase are also expressed. These findings allow a better understanding of the kinetic behavior of the enzymes that underlie the osmoregulatory mechanisms of euryhaline crustaceans.

Topics: Animals; Blotting, Western; Brachyura; Cations; Enzyme Activation; Gills; Kinetics; Nitrophenols; Organophosphorus Compounds; Ouabain; Phosphates; Potassium Compounds; Sodium Chloride; Sodium-Potassium-Exchanging ATPase; Water-Electrolyte Balance

The present study shows that when freezing nitrite containing biological samples in the presence of sodium and phosphate, a process of tyrosine nitration and S-nitrosocysteine formation is observed. The underlying mechanism is obviously based on the already described pH decrease in sodium phosphate buffered solutions during the freezing process and probably involves nitrous acid as an intermediate. However, in pure potassium phosphate buffer freeze-artefacts were absent. The yield of 3-nitrotyrosine from albumin-bound or free tyrosine depends not only on the concentration of nitrite, tyrosine or protein, and sodium phosphate but also on the velocity of the freezing process. Nitrite and nitrate were quantified by the Griess/nitrate reductase assay. 3-nitrotyrosine formation was quantitatively measured by HPLC analysis with optical and electrochemical detection as well as qualitatively investigated by immunohistochemistry and slot blot analysis using 3-nitrotyrosine specific antibodies. The formation of S-nitrosocysteine was detected by S-nitrosothiol specific antibodies and quantified by a fluorometric assay. Irrespective of the mechanism and although the here presented results cannot be generalized, the data warrant caution for the analysis of nitration or nitros(yl)ation products following freezing of nitrite containing biological material.

Topics: Animals; Aorta; Buffers; Cryopreservation; Cysteine; Freezing; Humans; Hydrogen-Ion Concentration; Nitrates; Nitric Oxide; Nitrites; Nitrophenols; Nitroso Compounds; Phosphates; Potassium Compounds; Rats; S-Nitrosothiols; Serum Albumin, Bovine; Tyrosine