Triphosphate Solution Research Articles

Spectral features of adenosine triphosphate solutions with calix[4]arene C-107

Spectral features of adenosine triphosphate solutions with calix[4]arene C-107

Fabrication and characterization of micro-band boron-doped diamond electrode for an application in adenosine phosphates sensor

Micro-band electrode was successfully fabricated by lamination method through sealing a piece of boron-doped diamond film inside a sandwich of two insulating plates, namely Teflon and silicon rubber as the gaskets. Characterization was performed using Raman and XPS spectra of the BDD film, while the fabricated micro-band was characterized by analyzing its SEM image. The electrode was examined for cyclic voltammetry of adenosine triphosphate solution, where an oxidation peak at +0.9 V vs. Ag/AgCl can be observed. The influence of scan rate and pH was also studied, in which pH 2 was selected as the optimum pH. The diffusion coefficient of 0.1 mM ATP at micro-band electrode was 3.84 x 10-8 m2/s, while the effective surface of the micro-band BDD electrode was 8.72 x 10-14 m2.

Proteins degradation value in cured meat product made from M. Cutaneous-omo brachialis muscle of bovine

We analyzed differences in some physicochemical parameters of proteins in shoulder rose (M. Cutaneous-omo brachialis) muscle as a result of beef processing to produce pastirma. Samples from processed muscles showed significantly increased concentrations of extracted proteins, especially of H2O P-ex and Guba-Straub–adenosine triphosphate solution (P < 0.01), as a result of the salting–curing process. The salt-curing process was likely to have an important effect on the extractability of muscle proteins such as myosin heavy chain (MHC) and water-soluble proteins, possibly as a result of releasing some proteins from each other and cleaving the structures between certain proteins. The fluorescence intensities of processed samples were higher than those of the control samples at all guanidine hydrochloride concentrations. The hydrophobicity also increased on account of new compounds that were created during the pastirma-making process. Since the process of making pastirma lasts about 4 weeks (drying), the metmyoglobin content was greatly increased in pastirma samples compared with the unprocessed samples (by as much as 57 %). Sodium dodecyl sulfate-polyacrylamide gel electrophoresis results conceived that during processing of pastirma products, MHC and other muscle proteins degraded into polypeptides with smaller molecular weight lower than 15-kDa. The results of this study demonstrated that meat processing promoted the enzymatic digestion of some proteins, and the differences in composition between the control and pastirma samples were thus likely to be owing to protein degradation. The traditional pastirma-making process hence has no negative impact on the structure of the muscle and produces a firmer-textured.

Preparation of titanium phosphates with additives in hydrothermal process and their powder properties for cosmetics

In this study, titanium phosphates were prepared from titanium chloride and phosphoric acid, sodium pyrophosphate and sodium triphosphate solutions with water retention compounds in hydrothermal process as a novel white pigment for cosmetics. Their chemical composition, powder properties, photo catalytic activity, water retention and smoothness were studied. The addition of glycerin in the preparation from sodium pyrophosphate has the useful method to obtain homogenized spherical particles of titanium phosphate pigments for the cosmetics. These titanium phosphates had less photo catalytic activity to protect the sebum on the skin.

Dielectric spectra broadening as a signature for dipole-matrix interaction. III. Water in adenosine monophosphate/adenosine-5′-triphosphate solutions

In this, the third part of our series on the dielectric spectrum symmetrical broadening of water, we consider the nucleotide aqueous solutions. Where in Parts I [E. Levy et al., J. Chem. Phys. 136, 114502 (2012)] and II [E. Levy et al., J. Chem. Phys. 136, 114503 (2012)], the dipole-dipole or ion-dipole interaction had a dominant feature, now the interplay between these two types of dipole-matrix interactions will be considered. We present the results of high frequency dielectric measurements of different concentrations of adenosine monophosphate/adenosine-5'-triphosphate aqueous solutions. We observed the Cole-Cole broadening of the main relaxation peak of the solvent in the solutions. Moreover, depending on the nucleotide concentration, we observed both types of dipole-matrix interaction. The 3D trajectory approach (described in detail in Part I) is applied in order to highlight the differences between the two types of interaction.

Preparation of Spherical and Balloonlike Calcium Phosphate Particles from Forced Hydrolysis of Ca(OH)2-Triphosphate Solution and Their Adsorption Selectivity of Water

The effects of addition of HCl on the formation of monodispersed spherical calcium hydroxyapatite (Hap) particles from the forced hydrolysis reaction of Ca(OH)2-triphosphate (tripolyphosphate, tpp: P3O105−) mixed solution were investigated. The fairly uniform spherical particles were formed at concentration of HCl (abbreviated as [HCl]) of 8−12 mM, but the particles with various shapes such as very small rodlike and/or large thin platelike were produced at high [HCl] region. These fairly uniform spherical particles produced only at [HCl] = 8−12 mM where the solution exhibited almost neutral pH of 6.89−7.24 after aging. The XRD patterns of the spherical particles as prepared were amorphous but they crystallized to β-Ca2P2O7 after the calcining the samples above 600 °C in air. The large amounts of H2O molecules were adsorbed on all the particles after evacuating the samples at 25 °C though they decreased drastically after evacuating the samples above 100 °C, except for the particles precipitated with a high...

Preparation and characterization of calcium hydroxyapatite and balloon-like calcium phosphate particles from forced hydrolysis of Ca(OH) 2–triphosphate solution

Calcium phosphate particles were prepared by aging a solution of dissolved Ca(OH) 2 and sodium triphosphate (sodium tripolyphosphate, Natpp: Na 5P 3O 10) at 100–150 °C for 18 h in a Teflon-lined screw-capped Pyrex test tube. Large spherical and/or small aggregated spherical particles were precipitated with an extremely fast rate of reaction under 100 °C. The large spherical particles were amorphous and the small aggregated ones were α-CaNa 2P 2O 7 .4H 2O. The former amorphous ones crystallized to β-Ca 2P 2O 7 after being calcined above 600 °C. Calcium hydroxyapatite (Ca 10(PO 4) 6(OH) 2, Hap), with rod-like and ellipsoidal or spherical aggregated shapes, was successfully produced using polyphosphates as a source of orthophosphate ions. Time resolved TEM measurement revealed that the crystallization of Hap particles takes place on the surface of tiny amorphous particles precipitated before aging. The tiny particles played the role of nuclei for Hap crystallization. The aging temperature drastically varied the particle shape under conditions for producing uniform amorphous spherical particles; solid spherical particles were produced with an aging temperature of up to 120 °C, whilst transparent balloon-like hollow spheres were precipitated at 125 °C. Finally, fully transparent balloon-like hollow spheres were produced with mere trace amounts of small rod-like particles after aging the solution above 127 °C. The time resolved TEM observation and ICP-AES measurements revealed that the balloon-like hollow spheres were produced by dissolving the interior of solid spherical particles after reinforcing their shell by the adsorption of unhydrolyzed tpp and/or pyrophosphate (pp) ions, which are the hydrolysis product of tpp. The balloon-like hollow spheres of calcium phosphate may have the potential use as drug delivery vehicles and have biocompatibility advantages.

Bone Morphogenetic Protein 4 Expressed in Esophagitis Induces a Columnar Phenotype in Esophageal Squamous Cells

Barrett's esophagus (BE) is a metaplastic condition in which normal squamous esophageal epithelium is replaced by columnar epithelium. It is proposed that one of the possible mechanisms is dedifferentiation of squamous epithelium into columnar epithelium. The pathophysiology through which this metaplasia occurs is unknown. A recent study by serial analysis of gene expression showed that bone morphogenetic protein 4 (BMP-4) is uniquely expressed in BE. In this study, the role of the BMP pathway in the metaplastic transformation of normal squamous cells into columnar cells was examined. Tissues from patients with esophagitis and BE and in an esophagitis-BE rat model were examined for the activation of the BMP pathway. Short-term cultures of primary normal squamous esophageal cells were treated with BMP-4, and cell biological changes were examined by Western blot analysis, immunohistochemistry, and microarrays. In both human and rat tissues, the BMP pathway proved to be activated in esophagitis and BE. Upon incubation of squamous cell cultures with BMP-4, the cytokeratin expression pattern showed a shift that was consistent with columnar epithelium. Involvement of the BMP pathway was suggested by up-regulation of Phosphorylated-Smad 1/5/8 (P-Smad 1/5/8) that was effectively blocked by Noggin, a BMP antagonist. Comparison of the gene expression profiles of squamous cells, BMP-4-treated squamous cells, and BE cells showed a significant shift in the profile of the BMP-4-treated squamous cells toward that of the cultured BE cells. These results suggest that the BMP pathway could play a role in the transformation of normal esophageal squamous cells into columnar cells.

EFFECT OF PHOSPHATE SALTS AND TRANSGLUTAMINASE IN PREVENTION OF FREEZE CRACKING IN FROZEN DICED BROILER BREAST

ABSTRACT Raw broiler breast meat was cooked and diced to 1.5 × 1.5 × 1.5 cm 3 then frozen under air‐blast, still‐air and cryogenic conditions. It was found that freezing with cryogenic at −70C at a rate of 37.50 cm/h produced 38.34% cracked pieces and increasing the freezing rate produced more cracked pieces. Cracking could be found on up to four sides of the dice. A small increase in the moisture of the dice drastically increased the cracking. Tumbling the meat with 1% sodium triphosphate solution prior to cooking and freezing at −70C reduced the amount of freeze cracking in the product from 47.50 to 24.17%. Tumbling the meat with 0.5% transglutaminase (TGase) reduced the cracked product to 25.84%. Increasing TGase not only increased the moisture content of the products but also reduced the number of cracked products. The TGase‐treated dices had narrower and shorter cracks than phosphate‐treated and without treatment dices.

Quantitative Investigation of the Effects of Chemical Decontamination Procedures on the Microbiological Status of Broiler Carcasses during Processing

The effects of elevated chlorine concentrations (25 ppm) added to water in the final carcass washing equipment on total viable counts (TVCs 22°C) and Escherichia coli and Enterobacteriaceae levels on poultry carcasses were investigated. Mean TVC counts on neck skin samples were significantly reduced when pre-evisceration and postwash samples were compared with log10 4.98 to 4.52 CFU/g recovered, respectively (P ≤ 0.05). No significant reductions in TVC counts were observed in control samples at corresponding sampling points subjected to wash water containing 1 to 2 ppm chlorine. E. coli and Enterobacteriaceae counts were not significantly altered following final carcass washing in the processing plant. A second trial assessed the microbial decontamination capabilities of sodium triphosphate (TSP) on broiler carcasses. Neck skin samples from carcasses were obtained before final washing (control), following a 15-s dip in potable water and after dipping in a 10% TSP solution (pH 12) for 15 s. Reductions in E. coli and Enterobacteriaceae counts were all statistically significant for both water and TSP-treated samples when compared with corresponding controls (P ≤ 0.01). The TSP treatment resulted in higher reductions of log10 1.95 and 1.86/g for E. coli and Enterobacteriaceae, respectively. In contrast, reductions of log10 0.37 and 0.31/g were observed for E. coli and Enterobacteriaceae counts when water-dipped carcasses were compared with corresponding controls. Significantly, Salmonella was not detected in any of the TSP-treated carcasses, while log10 1.92 and 1.04/g were found in control and water-dipped samples, respectively. Thermophilic Campylobacter counts were significantly lower in both treatment groups when compared with corresponding controls resulting in log10 0.55 and 1.71/g reductions for water- and TSP-dipped carcasses, respectively (P ≤ 0.01).

Fluorimetric trace determination of cerium(III) with sodium triphosphate

Sodium triphosphate acts as a specific reagent for enhancing the fluorescence intensity of cerium(III). The purpose of this study was to investigate the spectrofluorimetric determination of trace amounts of Ce(III) in sodium triphosphate solution. The excitation and emission wavelengths are 303.5 nm and 353 nm respectively. Optimum sodium triphosphate concentration is found to be 0.074 g l −1 at room temperature. The fluorescence varies linearly with the concentration of cerium(III) in the range 0.001–45 μg ml −1. The detection limit is 9.4 × 10 −4 μg ml −1. The relative standard deviations for 30 μg ml −1 and 0.05 μg ml −1 Ce(III) in 0.074 g l −1 sodium triphosphate solution are 1.1% and 0.72% respectively. Quenching effects of other lanthanides and some inorganic anions are described. This method is a direct and rapid analytical method for the determination of Ce(III) in rare earth mixtures and cerium concentrates.

Accumulation of technetium-99m methylene diphosphonate: Conditions affecting adsorption to hydroxyapatite

Experiments were carried out to explore the mechanism of technetium-99m methylene diphosphonate (99mTc-MDP) adsorption with various calcium compounds including hydroxyapatite powder. 99mTc-MDP adsorption to hydroxyapatite was markedly inhibited by the addition of either pyrophosphate or methylene diphosphonate (MDP). Moreover, adsorbed 99mTc-MDP was partly removed by rinsing with pyrophosphate solution. Adsorption was pH-dependent and was inhibited by univalent cations, adenosine triphosphate solution, and guanosine triphosphate. Adsorption was most apparent to hydroxyapatite and calcium pyrophosphate and was less marked for the other calcium compounds tested. It is suggested that 99mTc-MDP adsorption is affected by the hydroxyapatite crystalline structure and environmental factors such as pH and the presence of phosphates, calcium compounds, and various cations.

The kinetics of the autoxidation of ferrous ions in aqueous tripolyphosphate solutions.

Abstract The kinetics of the autoxidation of ferrous ions in tripolyphosphate solutions (pH 2–8) at an ionic strength of 0.20 m NaClO4 was studied using a spectrophotometric technique. The rate expression for the oxidation reaction is given by: d[Fe(III)]⁄dt=4kI[FeII(Htpp4−)][O2]+4kII[FeII(Htpp4−)2][O2], and 4kII found is to be 1.0×102 m−1 sec−1 at 15°C. The simultaneous reaction paths of FeII(Htpp4−)+O2\xrightarrowkIFeIII(Htpp4−)+O2- and FeII(Htpp4−)2+O2\xrightarrowkIIFeIII(Htpp4−)2+O2- are consistent with the results obtained. When there is an excess of the triphosphate solution in the pH range from 6 to 8, the latter may be the rate-determining step. The acceleration of the oxidation of the ferrous ions in the triphosphate solution may be due to the fact that the stabilization of the oxidation products, FeIII(Htpp4−) and FeIII(Htpp4−)2, is greater than that of the corresponding ferrous triphosphate complexes. As the activation parameters for the latter reaction, the experiments gave the values of ΔH\eweq∼10 kcal mol−1 and ΔS\eweq∼−25 cal mol−1. deg−1. The negative and relatively small value of the entropy of activation suggests that the activated complex is more extensively hydrated than is the ferrous complex of FeII(Htpp4−)2.

Action of Bis-dinitrophenyllysine on Muscle Fibers: EXPERIMENTS ON SOME CONTRACTION INHIBITORS

Abstract Contraction of glycerinated muscle fibers in adenosine triphosphate solution is inhibited by pretreatment for several hours in solutions of bis-(2,4-dinitrophenyl)lysine (bis-DNP-lysine) at concentrations greater than about 5 x 10-4 m at 20°, pH 7, and ionic strength 0.1. Contraction is also inhibited by solutions of bis-DNP-ornithine and, to some extent, by solutions of DNP-isoleucine, DNP-leucine, and e-N-DNP-lysine, although higher concentrations are needed. DNP-glycine, DNP-valine, DNP-glutamic acid, and 2, 4-dinitrophenol are ineffective under the same conditions. Solutions of bis-DNP-lysine also inhibit the contraction of actomyosin threads. Bis-DNP-lysine is readily absorbed from solution by fresh or glycerinated muscle fibers; at a concentration of 15 x 10-4m, about 30 moles are absorbed per 105 g of dry muscle. The extent of absorption increases with increasing bis-DNP-lysine concentration, and simple absorption equations are not obeyed. Absorption is increased after the fibers have been treated with sulfhydryl group reagents: most of the absorbed bis-DNP-lysine is readily removed by washing with buffer, but a proportion, which increases with increasing duration of treatment, is strongly retained. Fiber extensibility is greatly increased by treatment with bis-DNP-lysine. Prolonged treatment causes dissolution of some of the protein, and the fibers shrink. Electron micrographs suggest that during treatment the Z-line and the m-line are dissolved or altered. The effects of sodium deoxycholate and sodium lauryl sulfate on muscle fibers are similar to those of the inhibitory dinitrophenyl compounds. Other contraction inhibitors studied under the same conditions, viz. cetylpyridinium chloride, cetrimide, acridine orange, and various sulfhydryl group reagents, appear to act in a different way. It is suggested that bis-DNP-lysine inhibits muscle contraction by displacing accessible polypeptide chains of myosin that are essential for the contractile mechanism.

Action of ultraviolet radiation upon ciliary movement in Paramecium

1. 1. The effect of UV radiation upon ciliary movement of Paramecium multimicronucleatum was studied by ( a) recording photographically tracings before and during irradiation, of the pathway traversed by an animal during 7 sec; and ( b) by stroboscopic measurement of ciliary rate before and during irradiation. 2. 2. Both measurements showed that the first effect of irradiation is increased rate of ciliary movement. The increase in rate varied inversely with the intensity of UV radiation. The period of increased ciliary rate was dependent upon UV dose. 3. 3. The increased rate of ciliary beat induced by irradiation subsides and is followed by a decrease in rate until translational movement ceases. 4. 4. Adenosine triphosphate solutions did not accelerate ciliary movement slowed by UV treatment. 5. 5. UV irradiation induces not only a slowing in the beat of the cilia but also a change in pattern of movement of the Paramecium which is recorded in the photographic tracings. Differential UV action on the body cilia as against the oral groove cilia appears to explain the various patterns obtained. 6. 6. The data are related to the findings in the literature.

The effect of visible light on adenosine triphosphate solution

The quantity of inorganic phosphate which can be extracted at 37° from ammonium hydroxide-neutralised, tris-buffered, 2 m M ATP solution shows a periodic rise and fall by about 1%, following exposure to mixed visible light of 500 lux for 2 seconds. This periodicity does not occur with ATP solution at 23°, nor with Na 2HPO 4 solution at 37°. The phosphate extractable has a peak at 300 lux, and is less at less intensity of illumination. and at greater illumination up to 1000 lux.

The use of specific antibody in electron microscopy. III. Localization of antigens by the use of unmodified antibody.

Antibody staining was observed in the electron microscope by means of untagged antibody and osmium fixation. The antibody was visualized as a change in morphology due to its deposition on the antigenic structures. Glycerinated chicken breast muscle was stained with antimyosin, anti-H-meromyosin, and antiactin. The staining patterns obtained by electron microscopy were consistent with those previously demonstrated by fluorescence microscopy. A second method was used for confirmation of antibody staining. This consisted of extraction of unstained portions of the sarcomere with 0.6 M potassium iodide, 10(-4)M adenosine triphosphate solution. Stained regions of the sarcomere remained intact because of insolubility of the combined antigen and antibody.

Phosphates and polyphosphates of the rare earth elements—III Cerium(III) tripolyphosphates

The reaction between cerium(III) chloride and sodium triphosphate solutions has been discussed. Evidences have been obtained that cerium(III) and triphosphate ions form two insoluble compounds in which the ratios Ce 3+: P 3O 10 5− are respectively 5 : 3 and 1 : 1. With excess triphosphate ions a stable solution is obtained. The characteristic absorption spectrum of cerium(III) chloride solutions is changed upon addition of excess sodium triphosphate as a result of the formation of relatively stable complex species. A new maximum between 300–304 mμ is observed. By the method of continuous variations, the complex is formed in the ratio Ce 3+ : P 3O 10 5− = 1 : 2, in the pH range of 3·0–9·5.