scholarly journals Effect of combination of electrolyte and buffer on electrical production in fuel cell microbial system with Pseudomonas sp. in molasses substrate

2020 ◽  
Vol 211 ◽  
pp. 03001
Author(s):  
Maswati Baharuddin ◽  
Muh Rajib ◽  
Sappewali ◽  
Ummi Zahra
Keyword(s):  
Electrolyte Solution ◽  
Phosphate Buffer ◽  
Phosphate Buffer Solution ◽  
Potassium Phosphate ◽  
Salt Bridge ◽  
High Energy ◽  
Pseudomonas Sp ◽  
Buffer Solution ◽  
Sodium Phosphate Buffer ◽  
Potassium Phosphate Buffer Solution

MFC is a bio-electrochemical system driving an electric current by using high-energy bacteria and oxidants. This research aimed to investigate the effect of electrolyte and buffer on electrical production using Pseudomonas sp. In Molasses substrate. The method in this research was the double compartment that consist of anode and cathode chambers. Both were related by salt bridge. This study showed that the addition of a combination of KMnO4 electrolyte solution with sodium phosphate buffer solution obtained a maximum potential difference of 0.67 V. The result also revealed that the combination of KMnO4 electrolyte solution with Potassium Phosphate Buffer solution produced a 1.44 mA maximum current with power density of 660.82 mW/m2.

scholarly journals In-house validation method for quantification of amoxicillin in medicated feedingstuffs with the use of HPLC-DAD technique

2020 ◽  
Vol 64 (3) ◽  
pp. 433-438
Author(s):  
Ewelina Patyra ◽  
Krzysztof Kwiatek
Keyword(s):  
Phosphate Buffer ◽  
High Performance ◽  
Limit Of Detection ◽  
Phosphate Buffer Solution ◽  
Potassium Phosphate ◽  
High Performance Liquid Chromatographic ◽  
Array Detector ◽  
Buffer Solution ◽  
Limit Of Quantification ◽  
Potassium Phosphate Buffer Solution

AbstractIntroductionA high-performance liquid chromatographic–diode array detector (HPLC-DAD) method for the determination of amoxicillin in medicated feedingstuffs was developed and validated. The method was used to investigate the quality requirements of animal feedingstuffs (declared content of active substance and feed homogeneity).Material and MethodsTwo-gram samples were extracted by potassium phosphate buffer solution. Extracts were filtered and directly analysed by HPLC-DAD without further clean-up. Amoxicillin was separated by acetonitrile and 0.01M phosphate buffer (pH 5.0) on a Phenomenex Luna C18 column.ResultsThis method provided average recoveries of 76.1 to 81.6% with coefficients of variation (CV, %) for repeatability and reproducibility in the ranges of 3.7–7.2% and 5.3–7.6%, respectively. The limit of detection was 51.2 mg/kg and limit of quantification was 103.0 mg/kg.ConclusionThe method was successfully validated and proved to be efficient, precise, and useful for quantification of amoxicillin in medicated feedingstuffs.

scholarly journals THE PROPERTIES OF MAMMALIAN STRIATED MYOFIBRILS ISOLATED BY AN ENZYMATIC METHOD

1950 ◽  
Vol 91 (6) ◽  
pp. 655-664 ◽  
Author(s):  
Armin F. Schick ◽  
George M. Hass
Keyword(s):  
Ionic Strength ◽  
Potassium Chloride ◽  
Phosphate Buffer ◽  
Phosphate Buffer Solution ◽  
Potassium Phosphate ◽  
Microscopic Structure ◽  
Buffer Solution ◽  
Buffer Solutions ◽  
Alkaline Side ◽  
Fresh Frozen

A new method for the isolation of large numbers of individual myofibrils from fresh mammalian skeletal and cardiac muscle has been described. Purification of isolated myofibrils was accomplished by differential centrifugation of fresh frozen sections of muscle which had been mechanically agitated after exposure for 30 to 45 minutes at 0°C. to the action of a dilute solution of trypsin in a phosphate buffer solution with a pH of 7.0 and an ionic strength of 0.25. Isolated skeletal myofibrils of the rabbit and man have similar constant solubility properties. They dissolve in an aqueous mixture of 0.5 N potassium chloride and 0.03 N sodium bicarbonate, giving viscous solutions which exhibit conspicuous birefringence of flow. They are soluble in buffer solutions (ionic strength 0.15) on the acid side of pH 4 and alkaline side of pH 10. If the ionic strength of potassium phosphate buffer solutions is increased to 0.5 or if the ionic strength of phosphate-borate buffer solutions is increased to a similar value by addition of potassium chloride, the isolated myofibrils become soluble at neutrality. Hence, it is possible, first to isolate the myofibrils and then dissolve them without deviating appreciably from physiologic ranges of pH. The extent to which myofibrils are modified by the conditions imposed by the method of isolation is unknown. There is no significant change in microscopic structure or optical birefringence. Furthermore, there is retention of a form of physiological reactivity, for when the isolated skeletal myofibrils are immersed in solutions of adenosinetriphosphate, they promptly and irreversibly change from elongated fibrils with distinct structural detail into dense spherical masses without recognizable microscopic structure.

scholarly journals One-step synthesis of Ni(OH)2/MWCNT nanocomposites for constructing a nonenzymatic hydroquinone/O2 fuel cell

RSC Advances ◽  
2020 ◽  
Vol 10 (65) ◽  
pp. 39447-39454
Author(s):  
Yuan Wu ◽  
Xiaonan Yang ◽  
Shuhui Liu ◽  
Yonglei Xing ◽  
Juan Peng ◽  
...  
Keyword(s):  
Fuel Cell ◽  
Energy Density ◽  
Phosphate Buffer ◽  
Phosphate Buffer Solution ◽  
High Energy ◽  
Moderate Temperature ◽  
High Energy Density ◽  
Buffer Solution ◽  
One Step

In this work, a H-type hydroquinone/O2 fuel cell was assembled and shows high energy density in neutral phosphate buffer solution at moderate temperature.

scholarly journals SECOND-ORDER DERIVATIVE UV SPECTROPHOTOMETRIC AND RP-HPLC METHODS FOR THE ANALYSIS OF VILDAGLIPTIN AND APPLICATION FOR DISSOLUTION STUDY

2018 ◽  
Vol 2 (1) ◽  
pp. 46-53
Author(s):  
Amanda Thomas Barden ◽  
Bruna L Piccoli ◽  
Nadia Maria Volpato ◽  
Martin Steppe
Keyword(s):  
Phosphate Buffer Solution ◽  
Potassium Phosphate ◽  
Second Order ◽  
Order Derivative ◽  
Buffer Solution ◽  
Solution Ph ◽  
Zero Crossing ◽  
Dipeptidyl Peptidase 4 ◽  
Therapeutic Class ◽  
Potassium Phosphate Buffer Solution

This study describes two analytical methods, by second-order derivative UV spectrophotometric by HPLC, for determination of vildagliptin, a drug used for treatment of type 2 Diabetes Mellitus that belongs to a therapeutic class called inhibitors of dipeptidyl peptidase 4. The methods were validated in accordance with ICH and USP requirements. Analyses by UV derivative method were performed at 220 nm, which was the zero crossing point of excipient solutions. HPLC was optimized and the analysis was carried out using a Zorbax Eclipse Plus RP-C8 column (150 mm × 4.6 mm, 5 μm), detection at 207 nm, and potassium phosphate buffer solution pH 7.0 : acetonitrile (85:15, v/v) as mobile phase. In dissolution test, the conditions used were 0.01 mol L-1 hydrochloric acid in 900 mL of dissolution medium, USP apparatus 2 (paddle) and 50 rpm stirring speed. Both methods were successfully applied for analysis of dissolution samples from marketed vildagliptin tablets.

scholarly journals Crosslinking Efficacy and Cytotoxicity of Genipin and Its Activated Form Prepared by Warming It in a Phosphate Buffer: A Comparative Study

Materials ◽  
2021 ◽  
Vol 14 (21) ◽  
pp. 6600
Author(s):  
Takeya Kawamura ◽  
Shunji Yunoki ◽  
Yoshimi Ohyabu ◽  
Toshio Uraoka ◽  
Kazuaki Muramatsu
Keyword(s):  
Phosphate Buffer ◽  
Phosphate Buffer Solution ◽  
Mechanical Tests ◽  
Buffer Solution ◽  
Sodium Phosphate Buffer ◽  
In Situ Forming ◽  
Custom Made ◽  
Acute Cytotoxicity ◽  
Sodium Phosphate Buffer Solution

The aim of the present study was to compare the acute and cumulative cytotoxicity of intact (n-GE) and warmed genipin (w-GE), while investigating the differences in crosslinking capabilities of these two genipins by rheological and mechanical tests. The n-GE solution was prepared by dissolving genipin powder in a sodium phosphate buffer solution. The w-GE solution was prepared by warming the n-GE solution at 37 °C for 24 h. The mechanical tests for chitosan (CH)/genipin gels showed the crosslinking rate of w-GE was much greater than that of n-GE up until 6 h after preparation, whereas the degree of crosslinking of CH/n-GE gels became higher at 12 h. The ISO 10993-5 standard method, which is established specifically for evaluating cumulative cytotoxicity, determined equivalent IC50 for w-GE (0.173 mM) and n-GE (0.166 mM). On the other hand, custom-made cytotoxicity tests using a WST-8 assay after 1 h of cultivation showed that the acute cytotoxicity of w-GE was significantly higher than that of n-GE at concentrations between 0.1–5 mM. The acute cytotoxicity of w-GE should be taken into consideration in its practical uses, despite the fact that the much faster crosslinking of w-GE is useful as an effective cross linker for in-situ forming gels.

Biomechanical and biochemical changes in lumbar vertebrae of rapidly growing rats

1989 ◽  
Vol 256 (1) ◽  
pp. R259-R263 ◽  
Author(s):  
G. J. Salem ◽  
R. F. Zernicke ◽  
A. C. Vailas ◽  
D. A. Martinez
Keyword(s):  
Phosphate Buffer Solution ◽  
Lumbar Vertebrae ◽  
Potassium Phosphate ◽  
Bone Adaptation ◽  
Specimen Preparation ◽  
Buffer Solution ◽  
Test Protocol ◽  
Immature Rat ◽  
Vertebral Bone ◽  
Potassium Phosphate Buffer Solution

Although growth-related biochemical, morphological, and biomechanical properties of rat cortical bone have been investigated, similar properties of immature rat vertebral bone have not been well characterized. Information about these properties is necessary, however, for comparative analyses of rat vertebral bone adaptation. Thus a method was developed to characterize growth-related differences in immature rat vertebral bone. The centra of sixth lumbar vertebrae (L6) of 44-day-old and 54-day-old male Sprague-Dawley rats were compressed to 50% of their initial height at a 50%/s strain rate while immersed in a potassium phosphate buffer solution (pH 7.4, 37 degrees C). Structural and material properties for the 54-day-old group that were significantly greater than those for the 44-day-old group included load, stress, and energy at the proportional limit; initial maximum load and stress; and load and energy at 50% strain. The structural stiffness of L6, as well as its elastic modulus, was significantly greater in the older animals. The calcium concentrations and calcium-to-collagen ratios in 54-day-old vertebrae were significantly greater than in younger animals. These results indicated that the specimen preparation and testing protocol developed for rat vertebrae produced reliable biomechanical results, even with the relatively small size of rat vertebrae bodies, and that the quantity and quality of the matrix of immature rat vertebral bone changed significantly during this period of rapid growth. Our test protocol will be useful for investigating the responses of rat vertebral bone to exercise, disease, and spaceflight.

STUDIES ON THE AMOEBA-TO-FLAGELLATE TRANSFORMATION OF TETRAMITUS ROSTRATUS

1965 ◽  
Vol 11 (3) ◽  
pp. 441-446 ◽  
Author(s):  
Morgan M. Brent
Keyword(s):  
Bacterial Flora ◽  
Phosphate Buffer Solution ◽  
Potassium Phosphate ◽  
Potassium Phosphate Buffer ◽  
Buffer Solution ◽  
E Coli ◽  
Potassium Phosphate Buffer Solution ◽  
Factor Governing ◽  
Proportional Incidence ◽  
Peptone Broth

The amoebae of Tetramitus rostratus growing with Escherichia coli were inoculated into a yeast peptone broth and a potassium phosphate buffer solution, and flagellate formation was studied. In both, the numbers of flagellates formed and their proportional incidence increased with the number of amoebae inoculated. In buffer the numbers of flagellates reached a peak at 10 hours, and in broth at 23 hours.Comparisons between the buffer and broth, using the same inoculum, indicated that population density is only one factor governing flagellate formation, since this transformation was greater in buffer for a given population.Replacement of E. coli with four other monoxenic associates indicated that bacterial flora makes little difference in buffer on flagellate transformation, as flagellates were formed with all four genera. A search for a "flagellating substance" produced in the medium or within the cells was not successful.

scholarly journals Investigation of guanidine hydrochloride induced unfolding of apolipoprotein A-IMilano

2002 ◽  
Vol 16 (3-4) ◽  
pp. 199-206 ◽  
Author(s):  
Malin Suurkuusk ◽  
Dan Hallén
Keyword(s):  
Phosphate Buffer ◽  
Sodium Phosphate ◽  
Guanidine Hydrochloride ◽  
Phosphate Buffer Solution ◽  
Buffer Solution ◽  
Unfolded Protein ◽  
Sodium Phosphate Buffer ◽  
Apolipoprotein A ◽  
Helical Content ◽  
Sodium Phosphate Buffer Solution

A guanidine hydrochloride (GuHCl) induced unfolding study of apolipoprotein A-IMilano(apo A-IM) has been performed. The unfolding was followed by circular dichroism (CD) measurements at 222 nm and by isothermal titration (ITC) calorimetry at 25°C. In the ITC experiments enthalpies of transfer were determined for apo A-IMfrom aqueous sodium phosphate buffer solution into solutions of different concentrations of GuHCl. The CD data and the ITC data give complementary and consistent results of the complex unfolding process. Analytical ultracentrifugation experiments were made on apo A-IMin sodium phosphate buffer and in 0.6 M GuHCl, respectively. Analyses of the obtained sedimentation velocity data show that apo A-IMis highly aggregated in sodium phosphate buffer. The aggregates are almost completely dissociated in 0.6 M GuHCl. Aggregation of the protein in sodium phosphate buffer solution induces an increase in α-helical content. The loss of α-helical secondary structural element of the protein upon dissociation of the aggregates destabilises the protein resulting in a low GuHCl concentration of unfolding, [GuHCl]m=1.1 M. The unfolded protein has a significant α-helical content at the unfolded state. From ITC- and CD data we suggest that increased binding of GuHCl to the unfolded protein results in a disruption of the residual secondary structure.

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