Various Concentrations Of Ethylene Glycol Research Articles

Electrochemical Investigation of Ethylene Glycol as Corrosion Inhibitor of Al 5052

Nowadays, electric cars use Al 5052 in the cooling pad of the battery coolant system. Corrosion behavior study of Al 5052 by coolant is essential in the automotive industry. Ethylene glycol is the main compound of the battery coolant system that can inhibit the corrosion process of aluminum alloys. The corrosion inhibition performance of ethylene glycol (EG) for Al 5052 surface in 3.5% NaCl solution has been studied using electrochemical measurements such as potentiodynamic polarization and electrochemical impedance spectroscopy (EIS) in various concentrations of EG up to 50% and a temperature range from 30oC to 60oC. Based on results, EG can inhibit the corrosion process of Al 5052. The corrosion rate (CR) of coolant containing EG decreases with increasing that concentration in various temperatures, and the CR of the coolant rises with the increased temperatures. The inhibition efficiency of coolant boosts with the increase in EG concentration in each operational temperature and the highest up to 75% at 60oC with 50% of EG concentration.

Fabrication of Trimetallic Pt−Pd−Co Porous Nanostructures on Reduced Graphene Oxide by Galvanic Replacement: Application to Electrocatalytic Oxidation of Ethylene Glycol

AbstractIn present work, reduced graphene oxide nanosheets (rGO) decorated with trimetallic three‐dimensional (3D) Pt−Pd−Co porous nanostructures was fabricated on glassy carbon electrode (Pt−Pd−Co/rGO/GCE). First, GO suspension was drop‐casted on the electrode surface, then GO film reduction was carried out by cycling the potential in negative direction to form the rGO film modified GCE (rGO/GCE). Then, electrodeposition of the cobalt nanoparticles (CoNPs) as sacrificial seeds was performed onto the rGO/GCE by using cyclic voltammetry. Afterward, Pt−Pd−Co 3D porous nanostructures fabrication occurs through galvanic replacement (GR) method based on a spontaneous redox process between PtCl2, PdCl2, and CoNPs. The morphology and structure of the Pt−Pd−Co/rGO porous nanostructure film was characterized by scanning electron microscopy, energy dispersive spectroscopy and X‐ray diffraction method. The performance of the prepared electrode was investigated by various electrochemical methods including, cyclic voltammetry and electrochemical impedance spectroscopy. The electrocatalytic activity of the as‐prepared modified electrode with high surface areas was evaluated in anodic oxidation of ethylene glycol. The study on electrocatalytic performances revealed that, in comparison to various metal combinations in modified electrodes, trimetallic Pt−Pd−Co/rGO/GCE exhibit a lower onset potential, significantly higher peak current density, high durability and stability for the anodic oxidation of ethylene glycol. The excellent performances are attributed to the rGO as catalysts support and resulting synergistic effects of the trimetallic and appropriate characteristics of the resulted 3D porous nanostructures. Moreover, the influence of various concentrations of ethylene glycol, the potential scan rate and switching potential on the electrode reaction, in addition, long‐term stability have been studied by chronoamperometric and cyclic voltammetric methods.

Preliminary evaluation of a quantitative ethylene glycol test in dogs and cats

Ethylene glycol (EG) toxicity is commonly encountered in dogs and cats. The purpose of the current study was to determine if the Catachem test kit (Catachem Inc., Oxford, Connecticut) could precisely and accurately detect the presence of EG added to serum and plasma from 6 dogs and 4 cats. Serum and plasma samples were spiked at various concentrations of EG (0, 20, 60, and 100 mg/dl) and analyzed using the Catachem kit. Twenty randomly selected samples were also submitted for gas chromatography-mass spectroscopy (GC-MS) analysis of EG concentration, which was considered the gold standard. Inter- and intra-assay coefficients of variation (CVs) were calculated. Bland-Altman analysis was performed to compare the Catachem results to the GC-MS analyses. Analysis of serum samples showed a bias of 8.48 mg/dl (95% limits of agreement: 17.8 to -0.9 mg/dl) while spiked plasma samples had a bias of 7.32 mg/dl (18.1 to -3.5 mg/dl). Intra-assay CV was 0.7%. Interassay CV ranged from 1.2% to 2.0%. For all samples, the Catachem kit read higher than GC-MS values and slightly overestimated in vitro concentrations. The Catachem test kit is an accurate quantitative test for EG in dogs and cats that may aid in timely recognition of EG exposure. Because of the positive bias in all samples, some pets may receive treatment unnecessarily. However, animals with blood EG concentrations at or above the published lethal serum or plasma concentration will be readily identified so that treatment may be initiated.

PdNi-decorated manganite nanocatalyst for electrooxidation of ethylene glycol in alkaline media

PdNi bimetallic nanoparticles coated onto manganite (MN) nanocatalyst was used for ethylene glycol (EG) and glycerol (Gly) electrooxidation in alkaline media. The MN nanorods were prepared by hydrothermal method, and the PdNi was coated on the rods by an in situ reduction method. The prepared nanocomposite was characterized by scanning electron microscopy (SEM), Transmission Electron Microscopy (TEM), Energy dispersive X-ray spectroscopy (EDS), and electrochemical methods. The SEM and TEM images exhibit the formation of nanorods of 10 nm and also show the formation of nanocrystalline PdNi on the walls of the MN nanorods. This study shows that the MN nanorods can be excellent support material and they supply oxygen to the catalyst, by which the catalytic activity is enhanced. The electrooxidation reactions in strong alkaline condition containing various concentrations of EG have been studied. Among the different concentrations, 9 M KOH/6 M EG exhibits the highest activity. PdNi/MN nanocatalyst exhibits better activity even in higher electrolytic concentrations of EG and alkali.

Effect of ultrasound radiation on the size and size distribution of synthesized copper particles

The effect of ultrasound radiation on the size and size distribution of synthesized copper particles was investigated under various concentrations of ethylene glycol (E.G.) as a capping agent. Monodispersed copper particles were produced by the reduction of an aqueous copper (II) sulfate solution at the presence of hydrazine monohydrate. X-ray diffraction and scanning electron microscopy analysis revealed that the morphology, size, and size distribution of produced particles were influenced by the reducing agent injection rate, capping agent concentration, and sonication. Increasing the injection rate of reducing agent to an amount higher than a critical value decreases the size of copper particles and also converts the monodispersed particles to polydispersed particles. Results of using a sonifier at the reduction stage revealed that finer monodispersed copper particles can be achieved at higher injection rates related to the critical value. Increasing the concentration of E.G. as a capping agent decreases the size of copper particles, while applying ultrasound radiation along with increasing the concentration of E.G. increases the size of copper particles. Morphology of particles varies by the concentration and type of the capping agent. Higher reducing agent injection rates and the application of a sonifier at the instance of reduction result in smaller spherical particles at various capping agent concentrations.

Lowering intracellular and extracellular calcium contents prevents cytotoxic effects of ethylene glycol-based vitrification solution in unfertilized mouse oocytes.

We investigated the characteristics of the changes in intracellular calcium (Ca2+) concentration ([Ca2+](i)) and the viability of the unfertilized mouse oocytes exposed to various concentrations of ethylene glycol (EG)-containing solutions or vitrification solutions. Oocytes exposed to EG (1, 5, 10, 20, and 40% (v/v)) exhibited a rapid and dose-dependent increase in [Ca2+](i). The survival rate was 100% when oocytes were exposed to the EG concentration up to 5% through 5 min, while all oocytes were dead within 3 min when exposed to 10, 20, or 40% EG. When extracellular Ca2+ was removed, increase in [Ca2+](i) at 10 and 20% EG was less than that at the same concentrations of EG with extracellular Ca2+. The survival rates of the oocytes exposed to 10, 20, and 40% EG at 3 min were 100, 97, and 0%, respectively. In the presence of 20 microM 1,2-bis(o-aminopheoxy)ethane-N,N,N',N'-tetraacetic acid tetra acetoxymethyl ester (BAPTA-AM), a Ca2+ chelator, a small increase in [Ca2+](i) exposed to 10, 20, and 40% EG was observed until 4 min. Subsequently prolonged elevation of the [Ca2+](i) was observed in the oocytes exposed to 40% EG but not with 10 and 20% EG. The survival rate of the oocytes, in the presence of 20 microM BAPTA-AM, exposed to 10 and 20% EG was 100% throughout 5 min, while the oocytes exposed to 40% EG were alive only for 3 min. Treatment by the vitrification solution with various concentrations of EG (10, 20, and 40%) caused a smaller increase in [Ca2+](i), while the survival rates were higher compared to those without vitrification solution at the same concentrations of EG. These data suggested that the sustained [Ca2+](i) rises by EG in unfertilized mouse oocytes resulted in cell death. Therefore, the lowering of [Ca2+](i) in the oocytes exposed to the cryoprotectant may improve the viability of cryopreserved unfertilized oocytes.

Cryopreservation of Plant Mitochondria as a Tool for Protein Import or in Organello Protein Synthesis Studies.

Cryopreserved chloroplasts and thylakoids have recently been proven to be suitable for protein import and integration assays. The possibility of recovering intact plant mitochondria after storage would also facilitate a wide range of investigations that are currently underway on the molecular biology of these organelles, e.g. mitochondrial transcription, RNA editing, in organello protein synthesis, and protein or transfer RNA import. Therefore, we addressed the question whether cryopreservation of isolated plant mitochondria was also possible. Tobacco (Nicotiana tabacum) or broad bean (Vicia faba) mitochondria were quick frozen and stored in liquid nitrogen in the presence of various concentrations of ethylene glycol as a cryoprotectant. After thawing, up to 90% of the mitochondria stored in 5 to 10% ethylene glycol appeared to retain an intact outer membrane and normal oxidative phosphorylation activity. Their ultrastructural aspect, observed by electron microscopy, was similar to that of freshly prepared mitochondria. Furthermore, efficient in organello protein synthesis was carried out with mitochondria stored in the presence of 7.5% ethylene glycol. Finally, the precursor of the [beta] subunit of the mitochondrial F1-ATPase from Nicotiana plumbaginifolia was successfully translocated into V. faba cryopreserved mitochondria and processed. These data demonstrate that plant mitochondria cryopreserved under the conditions described here remain functional and can be used for a variety of physiological and biochemical studies.

Hydrophobic interaction chromatography of myosin fragments: Potential use in purification

Myosin fragments were fractionated on columns of the hydrophobic gel phenyl-Sepharose CL-4B. In the presence of high NaCl concentrations the fragments bound tightly to the columns; they could be eluted by decreasing the ionic strength, by increasing the pH, or by applying various concentrations of ethylene glycol. In myosin subfragment-1 (S-1), the light chains underwent partial dissociation from the heavy chain and bound separately to the column matrix. The order of strength of binding of the various species to the column was heavy chain > A1 light chain > A2 light chain > native S-1 > denatured heavy chain or S-1. Thus the hydrophobic gel appears to be able to differentiate between enzymatically active and inactive S-1. Under appropriate elution conditions it was possible to obtain S-1 preparations depleted from nicked heavy chains and with specific ATPase activities 34–130% higher than those of untreated S-1. When S-1(A2) was fractionated on phenyl-Sepharose a fivefold enrichment of the heavy chain with respect to the light chains was obtained, while the ATPase activity was equal or larger than that of the original S-1, implying that the light chains are not essential for ATPase activity. Thus, it seems that chromatography of S-1 on phenyl-Sepharose is a potentially useful method for obtaining a purified myosin heavy-chain fragment with a high ATPase specific activity.

Effect of cryoprotective agents on rat cutaneous nerves

Desheathed rat cutaneous nerves were exposed to various concentrations of ethylene glycol (EG), glycerol and dimethyl sulfoxide (DMSO) at temperatures of 1, 24, and 38 °C for periods of time ranging from 5 to 60 min. Measurements of the percent recovery of the original action potential (AP) were determined after removal of the cryoprotective agent (CPA) under various conditions, i.e., temperature, time and sequence of rinsing. A comparison of the results obtained after the nerves were exposed directly to a 15% concentration of the three CPAs at 1 °C for a 15-min period showed that the percentage of recovery of the AP was 90, 69, and 36% of the original values when treated with DMSO, EG, or glycerol, respectively. In all three groups, the nerves were rinsed at 1 °C for 15 min. If the exposure to glycerol at 1 °C was carried out in a gradual stepwise manner, the recovery of the AP in 10 and 15% solutions ranged from 58 to 64%. If the temperatures of the exposure and rinse were increased to 24 and 38 °C, glycerol produced some toxicity within 10 min and after 25 min no recovery of AP was obtained. The results of a 10-min direct exposure to EG at 1 °C showed a moderate decrease in recovery of the AP as the concentration was increased from 10 to 15–20%. Increasing the exposure time to 15 and 30 min at 1 °C also contributed to further reduction in recovery. DMSO, however, in concentrations of 10, 15, and 20% produced only a slight decline of AP after a 5–15 min exposure at 1 °C. Recovery ranged from 96% after 10 min in a 10% solution to 88% after 15 min in a 20% solution. Toxicity became more apparent with DMSO when nerves were exposed to 30% concentrations for 5–10 min; the latter time resulted in a 49% recovery of the AP. Exposure of nerves to a CPA solution containing isotonic concentrations of electrolytes resulted in a 10–30% improvement in recovery when compared with specimens treated with lower levels of salt. The effect of raising the temperature of the rinse to 38 °C and increasing the wash time to 20 min was studied in a few selected experiments. After a direct 15-min exposure to a 15% solution of a CPA at 1 °C the recovery in the case of glycerol was significantly increased with such treatment whereas with EG and DMSO it remained unchanged. There was no evidence of thermal or cold shock in this work.

Studies on new intracellular proteases in various organs of rat. 2. Mode of limited proteolysis.

1. The mechanism of proteolysis of ornithine transaminase apoenzyme II by group-specific protease and the relation between the confirmations of ornithine transaminase and its susceptibility to group-specific protease were studied to elucidate the mode of action of the protease. 2. Differences in the conformations of ornithine transaminase apoenzyme II, molecular weight 67000, and ornithine transaminase holoenzyme, molecular weight 140000, were shown by studies on difference spectra produced by various concentrations of ethylene glycol. Increase of the titratable sulfhydryl groups on resolution of the coenzyme from ornithine transaminase also supports this finding. These results are consistent with the facts that the apoenzyme was sensitive to group-specific protease, while the holoenzyme was not. 3. Kinetics studies showed that ornithine transaminase apoenzyme II was degraded by limited proteolysis. Reaction of the native enzyme with group-specific protease resulted in a nick in the enzyme molecule with formation of one homogeneous large product and small peptides. The large product was not degraded further. The large product was indistinguishable from native ornithine transaminase apoenzyme II in various properties including its elution volume on gel filtration, its mobility on disc electrophoresis, its antigenicity, its estimated number of exposed tryptophan residues, and its titratable number of sulfhydryl groups. But unlike the apoenzyme the product did not show tetramerization with coenzyme or catalytic activity, although it retained the ability to bind with coenzyme and had the same number of bound pyridoxal phosphate as the native ornithine transaminase molecule. Thus, native ornithine transaminase apoenzyme II was degraded by limited proteolysis. Unfolded enzyme, denatured by 8 M urea, was degraded extensively. 4. The initial step of intracellular proteins degradation is discussed on the basis of these results.