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Potassium carbonate

Potassium carbonate, a crystalline white salt with the chemical formula K2CO3, is a widely used compound in various industrial and commercial applications.
It is a key ingredient in the production of glass, ceramics, and fertilizers, and is also employed in the manufacture of soap, detergents, and pharmaceuticals.
Potassium carbonate is known for its ability to act as a pH regulator, buffer, and desiccant, making it a versatile chemical in numerous processes.
Researchers and scientists continue to explore the diverse applications and optimize the efficacy of potassium carbonate through rigorous experimentation and analysis.
This MeSH term provides a concise overview of the important properteis and uses of this essential chemical compund.

Most cited protocols related to «Potassium carbonate»

Antioxidant (DPPH and ABTS radical scavenging, reducing power (CUPRAC and FRAP), phosphomolybdenum, and metal chelating (ferrozine method)) and enzyme inhibitory activities [cholinesterase (ChE) Elmann’s method], tyrosinase (dopachrome method), α-amylase (iodine/potassium iodide method), and α -glucosidase (chromogenic PNPG method)) were determined using the methods previously described by Zengin et al. (2014) (link) and Dezsi et al. (2015) (link).
For the DPPH (1,1-diphenyl-2-picrylhydrazyl) radical scavenging assay: Sample solution (1 mg/mL; 1 mL) was added to 4 mL of a 0.004% methanol solution of DPPH. The sample absorbance was read at 517 nm after a 30 min incubation at room temperature in the dark. DPPH radical scavenging activity was expressed as millimoles of trolox equivalents (mg TE/g extract).
For ABTS (2,2′-azino-bis(3-ethylbenzothiazoline) 6-sulfonic acid) radical scavenging assay: Briefly, ABTS+ was produced directly by reacting 7 mM ABTS solution with 2.45 mM potassium persulfate and allowing the mixture to stand for 12–16 in the dark at room temperature. Prior to beginning the assay, ABTS solution was diluted with methanol to an absorbance of 0.700 ± 0.02 at 734 nm. Sample solution (1 mg/mL; 1 mL) was added to ABTS solution (2 mL) and mixed. The sample absorbance was read at 734 nm after a 30 min incubation at room temperature. The ABTS radical scavenging activity was expressed as millimoles of trolox equivalents (mmol TE/g extract) (Mocan et al., 2016a (link)).
For CUPRAC (cupric ion reducing activity) activity assay: Sample solution (1 mg/mL; 0.5 mL) was added to premixed reaction mixture containing CuCl2 (1 mL, 10 mM), neocuproine (1 mL, 7.5 mM) and NH4Ac buffer (1 mL, 1 M, pH 7.0). Similarly, a blank was prepared by adding sample solution (0.5 mL) to premixed reaction mixture (3 mL) without CuCl2. Then, the sample and blank absorbances were read at 450 nm after a 30 min incubation at room temperature. The absorbance of the blank was subtracted from that of the sample. CUPRAC activity was expressed as milligrams of trolox equivalents (mg TE/g extract).
For FRAP (ferric reducing antioxidant power) activity assay: Sample solution (1 mg/mL; 0.1 mL) was added to premixed FRAP reagent (2 mL) containing acetate buffer (0.3 M, pH 3.6), 2,4,6-tris(2-pyridyl)-S-triazine (TPTZ) (10 mM) in 40 mM HCl and ferric chloride (20 mM) in a ratio of 10:1:1 (v/v/v). Then, the sample absorbance was read at 593 nm after a 30 min incubation at room temperature. FRAP activity was expressed as milligrams of trolox equivalents (mg TE/g extract).
For phosphomolybdenum method: Sample solution (1 mg/mL; 0.3 mL) was combined with 3 mL of reagent solution (0.6 M sulfuric acid, 28 mM sodium phosphate and 4 mM ammonium molybdate). The sample absorbance was read at 695 nm after a 90 min incubation at 95°C. The total antioxidant capacity was expressed as millimoles of trolox equivalents (mmol TE/g extract) (Mocan et al., 2016c (link)).
For metal chelating activity assay: Briefly, sample solution (1 mg/mL; 2 mL) was added to FeCl2 solution (0.05 mL, 2 mM). The reaction was initiated by the addition of 5 mM ferrozine (0.2 mL). Similarly, a blank was prepared by adding sample solution (2 mL) to FeCl2 solution (0.05 mL, 2 mM) and water (0.2 mL) without ferrozine. Then, the sample and blank absorbances were read at 562 nm after 10 min incubation at room temperature. The absorbance of the blank was sub-tracted from that of the sample. The metal chelating activity was expressed as milligrams of EDTA (disodium edetate) equivalents (mg EDTAE/g extract).
For ChE inhibitory activity assay: Sample solution (1 mg/mL; 50 μL) was mixed with DTNB (5,5-dithio-bis(2-nitrobenzoic) acid, Sigma, St. Louis, MO, United States) (125 μL) and AChE [acetylcholines-terase (Electric ell AChE, Type-VI-S, EC 3.1.1.7, Sigma)], or BChE [BChE (horse serum BChE, EC 3.1.1.8, Sigma)] solution (25 μL) in Tris–HCl buffer (pH 8.0) in a 96-well microplate and incubated for 15 min at 25°C. The reaction was then initiated with the addition of acetylthiocholine iodide (ATCI, Sigma) or butyrylthiocholine chloride (BTCl, Sigma) (25 μL). Similarly, a blank was prepared by adding sample solution to all reaction reagents without enzyme (AChE or BChE) solution. The sample and blank absorbances were read at 405 nm after 10 min incubation at 25°C. The absorbance of the blank was subtracted from that of the sample and the cholinesterase inhibitory activity was expressed as galanthamine equivalents (mgGALAE/g extract) (Mocan et al., 2016b (link)).
For Tyrosinase inhibitory activity assay: Sample solution (1 mg/mL; 25 μL) was mixed with tyrosinase solution (40 μL, Sigma) and phosphate buffer (100 μL, pH 6.8) in a 96-well microplate and incubated for 15 min at 25°C. The reaction was then initiated with the addition of L-DOPA (40 μL, Sigma). Similarly, a blank was prepared by adding sample solution to all reaction reagents without enzyme (tyrosinase) solution. The sample and blank absorbances were read at 492 nm after a 10 min incubation at 25°C. The absorbance of the blank was subtracted from that of the sample and the tyrosinase inhibitory activity was expressed as kojic acid equivalents (mgKAE/g extract) (Mocan et al., 2017 (link)).
For α-amylase inhibitory activity assay: Sample solution (1 mg/mL; 25 μL) was mixed with α-amylase solution (ex-porcine pancreas, EC 3.2.1.1, Sigma) (50 μL) in phosphate buffer (pH 6.9 with 6 mM sodium chloride) in a 96-well microplate and incubated for 10 min at 37°C. After pre-incubation, the reaction was initiated with the addition of starch solution (50 μL, 0.05%). Similarly, a blank was prepared by adding sample solution to all reaction reagents without enzyme (α-amylase) solution. The reaction mixture was incubated 10 min at 37°C. The reaction was then stopped with the addition of HCl (25 μL, 1 M). This was followed by addition of the iodine-potassium iodide solution (100 μL). The sample and blank absorbances were read at 630 nm. The absorbance of the blank was subtracted from that of the sample and the α-amylase inhibitory activity was expressed as acarbose equivalents (mmol ACE/g extract) (Savran et al., 2016 (link)).
For α-glucosidase inhibitory activity assay: Sample solution (1 mg/mL; 50 μL) was mixed with glutathione (50 μL), α-glucosidase solution (from Saccharomyces cerevisiae, EC 3.2.1.20, Sigma) (50 μL) in phosphate buffer (pH 6.8) and PNPG (4-N-trophenyl-α-D-glucopyranoside, Sigma) (50 μL) in a 96-well microplate and incubated for 15 min at 37°C. Similarly, a blank was prepared by adding sample solution to all reaction reagents without enzyme (α-glucosidase) solution. The reaction was then stopped with the addition of sodium carbonate (50 μL, 0.2 M). The sample and blank absorbances were read at 400 nm. The absorbance of the blank was subtracted from that of the sample and the α-glucosidase inhibitory activity was expressed as acarbose equivalents (mmol ACE/g extract) (Llorent-Martínez et al., 2016 (link)).
All the assays were carried out in triplicate. The results are expressed as mean values and standard deviation (SD). The differences between the different extracts were analyzed using one-way analysis of variance (ANOVA) followed by Tukey’s honestly significant difference post hoc test with α = 0.05. This treatment was carried out using SPSS v. 14.0 program.
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Publication 2017
Protein concentration was determined using a BCA assay (Pierce). The indicated amounts of antibodies and lysates were incubated for 1 h, after that 10 to 25 μl protein G agarose beads (Immobilized Protein G, Pierce) were added and immunoprecipitation was performed overnight. All steps were performed with mild agitation at 4°C. For mass spectrometric analysis, lysates were precleared by incubation with the same amount of beads for 2 h before the antibody was added. The supernatants of the immunoprecipitations were kept for analysis and the beads were washed either twice with PBS for western blot analysis or three times with RIPA buffer for mass spectrometric analysis. 4x reducing SDS Loading Dye (500 mM Tris HCl, pH 6.8, 8% SDS, 40% glycerine, 20% β-mercaptoethanol, 5 mg/ml bromophenol blue) was added to the beads as well as to the lysates and the supernatants and samples were incubated at either 65°C or 99°C for 5 min or 10–20 min, respectively, before they were separated by SDS PAGE using a 8% Laemmli gel [19 (link)]. For western blot analysis, proteins were transferred via a semi-dry procedure on polyvinylidene difluoride membranes (Pall Corporation), blocked for 1 h at RT with 5% milk powder in PBST (PBS, 0.1% Tween 20) and incubated with JB1A (0.1 μg/ml) overnight at 4°C. Membranes were either incubated with anti-mouse HRP or anti-mouse Alexa Fluor 680 (both 1 : 10000) for 1 h at RT. Membranes treated with anti-mouse Alexa Fluor 680 were scanned with a fluorescence scanner (Odyssey, LICOR) using excitation/emission wavelengths of 700 and 800 nm, whereas signals on anti-mouse HRP incubated membranes were detected with chemiluminescence solution (ECL, GE Healthcare). Quantitation of immunoblot analysis was performed using the software ImageJ [20 ]. Silver staining was performed using a modified protocol of Gharahdaghi et al. [21 (link)]. Briefly, gels were fixed with 10% acetic acid/10% methanol, washed with water and sensitized with 1 μg/ml dithiothreitol for 15 min. Gels were incubated in 0.1% (w/v) silver nitrate for 15 min and developed with 0.02% (w/v) paraformaldehyde in 3% (w/v) potassium carbonate until the desired staining had occurred. The reaction was stopped by addition of acetic acid.
Publication 2010
2-Mercaptoethanol Acetic Acid Antibodies Biological Assay Bromphenol Blue Buffers Chemiluminescence Dithiothreitol Fluorescence G-substrate Gels Glycerin Immunoblotting Immunoglobulins Immunoprecipitation Mass Spectrometry Methanol Mice, House Milk, Cow's paraform polyvinylidene fluoride potassium carbonate Powder Proteins Radioimmunoprecipitation Assay SDS-PAGE Sepharose Silver Nitrate Tissue, Membrane Tromethamine Tween 20 Western Blot
Agarose-normal melting (molecular biology grade-MB), agarose-low melting (MB), sodium chloride (analytical reagent grade-AR), potassium chloride (AR), disodium hydrogen phosphate (AR), potassium dihydrogen phosphate (AR), disodium ethylenediaminetetraacetic acid (disodium EDTA) (AR), tris (AR), sodium hydroxide (AR), sodium dodecyl sulphate / sodium lauryl sarcosinate (AR), tritron X 100 (MB), trichloro acetic acid, zinc sulphate (AR), glycerol (AR), sodium carbonate (AR), silver nitrate (AR), ammonium nitrate (AR), silicotungstic acid (AR), formaldehyde (AR) and lymphocyte separation media (Ficoll/ Histopaque 1077 [Sigma]/ HiSep [Himeda]).
Publication 2011
ammonium nitrate dodecyl sulfate Edetic Acid Ficoll Formaldehyde Glycerin histopaque Lymphocyte Potassium Chloride potassium phosphate, monobasic Sepharose silicotungstic acid Silver Nitrate sodium carbonate Sodium Chloride Sodium Hydroxide sodium phosphate, dibasic Sodium Sarcosinate Trichloroacetic Acid Tromethamine Zinc Sulfate
Determination of total phenolic content (TPC): Amount of TP were assessed using the Folin-Ciocalteu reagent [25 ]. Briefly, the crude extract (50 mg) was mixed with Folin-Ciocalteu reagent (0.5 mL) and deionized water (7.5 mL). The mixture was kept at room temperature for 10 min, and then 20% sodium carbonate (w/v, 1.5 mL) was added. The mixture was heated in a water bath at 40 oC for 20 min and then cooled in an ice bath; absorbance was read at 755 nm using a spectrophotometer (U-2001, Hitachi Instruments Inc., Tokyo, Japan). Amounts of TP were calculated using gallic acid calibration curve within range of 10-100 mgL-1(R2 = 0.9986). The results were expressed as gallic acid equivalents (GAE) g/100g of dry plant matter. All samples were analyzed thrice and the results averaged. The results are reported on dry weight basis (DW).
Determination of total flavonoid contents (TFC): The TFC were measured following a previously reported spectrophotometric method [26 (link)]. Briefly, extracts of each plant material (1 mL containing 0.1 mg/mL) were diluted with water (4 mL) in a 10 mL volumetric flask. Initially, 5% NaNO2 solution (0.3 mL) was added to each volumetric flask; at 5 min, 10% AlCl3 (0.3 mL) was added; and at 6 min, 1.0 M NaOH (2 mL) was added. Water (2.4 mL) was then added to the reaction flask and mixed well. Absorbance of the reaction mixture was read at 510 nm. TFC were determined as catechin equivalents (g/100g of dry weight). Three readings were taken for each sample and the results averaged.
Determination of reducing power: The reducing power of the extracts was determined according to the procedure described earlier [27 ], with a slight modification. Concentrated extract (2.5-10.0 mg) was mixed with sodium phosphate buffer (5.0 mL, 0.2 M, pH 6.6) and potassium ferricyanide (5.0 mL, 1.0%); the mixture was incubated at 50 oC for 20 min. Then 10% trichloroacetic acid (5 mL) was added and the mixture centrifuged at 980 g for 10 min at 5 °C in a refrigerated centrifuge (CHM-17; Kokusan Denki, Tokyo, Japan). The upper layer of the solution (5.0 mL) was decanted and diluted with 5.0 mL of distilled water and ferric chloride (1.0 mL, 0.1%), and absorbance read at 700 nm using a spectrophotometer (U-2001, Hitachi Instruments Inc., Tokyo, Japan). All samples were analyzed thrice and the results averaged.
DPPH. scavenging assay: 1, 1–diphenyl–2-picrylhydrazyl (DPPH) free radical scavenging activity of the extracts was assessed using the procedure reported earlier [28 (link)]. Briefly, to extract (1.0 mL) containing 25 μg/mL of dry matter in methanol, freshly prepared solution of DPPH (0.025 g/L, 5.0 mL) was added. Absorbance at 0, 0.5, 1, 2, 5 and 10 min was measured at 515 nm using a spectrophotometer. The scavenging amounts of DPPH radical (DPPH.) was calculated from a calibration curve. Absorbance read at the 5th min was used for comparison of radical scavenging activity of the extracts.
Determination of antioxidant activity in linoleic acid system: The antioxidant activity of the tested plant extracts was also determined by measuring the oxidation of linoleic acid [28 (link)]. Five mg of each plant extract were added separately to a solution of linoleic acid (0.13 mL), 99.8% ethanol (10 mL) and 0.2 M sodium phosphate buffer (pH 7, 10 mL). The mixture was made up to 25 mL with distilled water and incubated at 40 oC up to 360 h. Extent of oxidation was measured by peroxide value applying thiocyanate method as described by Yen et al. [27 ]. Briefly, ethanol (75% v/v, 10 mL ), aqueous solution of ammonium thiocyanate (30% w/v, 0.2 mL), sample solution (0.2 mL) and ferrous chloride (FeCl2) solution (20 mM in 3.5% HCl; v/v, 0.2 mL) were added sequentially. After 3 min of stirring, the absorption was measured at 500 nm using a spectrophotometer (U-2001, Hitachi Instruments Inc., Tokyo, Japan). A control contained all reagents with exception of extracts. Synthetic antioxidants butylated hydroxytoluene (BHT) was used as a positive control. Percent inhibition of linoleic acid oxidation was calculated with the following equation: 100 – [(increase in absorbance of sample at 360 h / increase in absorbance of control at 360 h) × 100], to express antioxidant activity.
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Publication 2009
Initial in vitro screening of the enzyme activity against (−)-cocaine was carried out by using a single concentration (1 mM) of (−)-cocaine, assuming that KM << 1 mM such that the enzyme was always saturated by 1 mM (−)-cocaine and the maximum reaction velocity (Vmax) was reached for a given concentration [E] of the enzyme. Vmax = kcat[E]. The relative concentrations of the enzymes were determined by using an enzyme-linked immunosorbent assay (ELISA)26 (link),52 (link) described below. The ELISA buffers used in the present study are the same as those described in literature.26 (link),52 (link) Specifically, the coating buffer was 0.1 M sodium carbonate/bicarbonate buffer (pH 9.5). The washing buffer (PBS-T) was 0.01 M potassium phosphate monobasic/potassium phosphate monohydrate buffer (pH 7.5) containing 0.05% (vol/vol) Tween 20. The diluent buffer (EIA buffer) was potassium phosphate monobasic/potassium phosphate monohydrate buffer (pH 7.5) containing 0.9% sodium chloride and 0.1% bovine serum albumin (BSA).
To measure (−)-cocaine and benzoic acid, the product of the enzymatic (−)-cocaine hydrolysis, we used sensitive radiometric assays based on toluene extraction of [3H](−)-cocaine labeled on its benzene ring.24 (link) In brief, to initiate the enzymatic reaction, 100 nCi of [3H](−)-cocaine was mixed with 100 µl of enzyme solution. For Michaelis-Menten kinetic analysis, the enzymatic reactions proceeded at 37°C and pH 8 with varying concentrations of (−)-cocaine. The reactions were stopped by adding 200 µl of 0.05 M HCl, which neutralized the liberated benzoic acid while ensuring a positive charge on the residual (−)-cocaine. [3H]benzoic acid was extracted by 1 ml of toluene and measured by scintillation counting. Finally, the measured (−)-cocaine concentration-dependent radiometric data were analyzed in terms of the standard Michaelis-Menten kinetics so that the catalytic parameters were determined. The enzyme activity assays with [3H]ACh were similar to the assays with [3H](−)-cocaine. The primary difference was that the enzymatic reaction was stopped by addition of 200 µl of 0.2 M HCl containing 2 M NaCl and that the product was [3H]acetic acid for the ACh hydrolysis.
Publication 2014
Acetic Acid Benzene Benzoic Acid Bicarbonate, Sodium Bicarbonates Biological Assay Buffers Carbonates Catalysis Cocaine Enzyme-Linked Immunosorbent Assay enzyme activity Enzyme Assays Enzymes Hydrolysis Kinetics M-200 potassium phosphate potassium phosphate, monobasic Radiometry Serum Albumin, Bovine sodium carbonate Sodium Chloride Toluene Tween 20

Most recents protocols related to «Potassium carbonate»

Potassium carbonate (250 mg,1.8 mmol) was suspended in acetonitrile, and A2 was added to it. One equivalent of propargyl bromide (1.8 mmol) was added and a catalytic amount of potassium iodide (0.1 equivalents) was added to the reaction mixture. The reaction was refluxed at 90 °C overnight. The reaction was filtered to remove excess potassium carbonate, and acetonitrile was removed under vacuum. Water was added to the mixture, then the product was extracted in dichloromethane twice. The combined organic phases were washed with brine and dried over anhydrous sodium sulfate to yield A3 (85% yield). The alternate route for A3 synthesis was obtained by modifying a literature method [34 (link)]. Commercially available 2-(chloromethyl)-1,3-benzthiazole was reacted with propargyl amine in the presence of a catalytic amount of potassium iodide and 3 equivalents of potassium carbonate in acetonitrile under reflux condition for 12 h. The product intermediate was isolated using solvent extraction to yield A3.
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Publication 2024
All reagents used in the synthesis and experimental processes were not further purified. Potassium carbonate (K2CO3), potassium bicarbonate (KHCO3), lithium carbonate (Li2CO3), and titanium dioxide (TiO2, Rutile) were purchased from Alfa Aesar. Ruthenium oxide (RuO2) was from Acros. Tetrabutylammonium hydroxide (TBAOH) and the ammonium ion standard solution (1000 μg/mL) were purchased from Shanghai Aladdin Biochemical Technology Co., Ltd. (Shanghai, China).
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Publication 2024
HCFU was purchased from BioNet, UK, and 5-FU
was received as a gift from JSC Grindex. HBA, potassium carbonate,
potassium iodide, and methanol were commercially available and used
without further purification.
Publication 2024
To examine antimicrobial efficacy, four groups were formed: three that were cleaned using alkaline peroxide cleanser tablets and a control group cleaned by immersion in distilled water (n = 5). The tablets were reprepared daily with distilled water according to the manufacturers’ instructions. The manufacturers and usage details of the tablets are presented in Table 3.

Cleanser tablets used in the study and their ingredients

Cleanser TabletManufacturerContentPreparation adviceContact Time
Corega™

GlaxoSmithKline Healthcare.

Istanbul. Turkey

Sodium bicarbonate. citric acid. potassium monopersulfate. sodium carbonate. sodium carbonate peroxide. TAED. sodium benzoate. PEG-180. sodium lauryl sulfoacetate. sodium perborate monohydrate VP/VA copolymer. flavor. subtilisin1 tablet with 200 ml water15 min
Aktident™

Aktif Dis Ticaret.

Istanbul

Potassium caroate. sodium bicarbonate. citric acid. sodium carbonate. sodium lauryl sulfate. sodium lauryl sulfoacetate. flavor1 tablet with 200 ml water15 min
Protefix™Quiesser Pharma. Flensburg. GermanySodium bicarbonate. Potassium carbonate. Sodium perborate. Citric acid. Sodium lauryl sulfate. Flavor1 tablet with 100 ml water10 min
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Publication 2024
The mineral phase transformation for FA was conducted in muffle furnace. FA was dried first and then mixed with Na2CO3 and/or K2CO3 respectively via a planetary ball mill for 2 h. The sample was calcined in the muffle furnace at the designed temperature for 2 h and cooled to room temperature to obtain activated fly ash. To study the effect of alkali metal cations on the mineral phase transformation for fly ash, three systems including fly ash–sodium carbonate (FN), fly ash–potassium carbonate (FK) and fly ash–sodium carbonate–potassium carbonate (FNK) were carried out. The addition of Na2CO3 in FN was 40% and the calcination temperatures was varied from 600 °C to 1200 °C. The addition of K2CO3 in FK was 50% and the calcination temperatures was from 600 °C to 1100 °C. The experimental conditions of FNK are shown in Table S1.
Publication 2024

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Gallic acid is a naturally occurring organic compound that can be used as a laboratory reagent. It is a white to light tan crystalline solid with the chemical formula C6H2(OH)3COOH. Gallic acid is commonly used in various analytical and research applications.
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Sodium carbonate is a water-soluble inorganic compound with the chemical formula Na2CO3. It is a white, crystalline solid that is commonly used as a pH regulator, water softener, and cleaning agent in various industrial and laboratory applications.
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DPPH is a chemical compound used as a free radical scavenger in various analytical techniques. It is commonly used to assess the antioxidant activity of substances. The core function of DPPH is to serve as a stable free radical that can be reduced, resulting in a color change that can be measured spectrophotometrically.
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Sodium hydroxide is a chemical compound with the formula NaOH. It is a white, odorless, crystalline solid that is highly soluble in water and is a strong base. It is commonly used in various laboratory applications as a reagent.
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Methanol is a clear, colorless, and flammable liquid that is widely used in various industrial and laboratory applications. It serves as a solvent, fuel, and chemical intermediate. Methanol has a simple chemical formula of CH3OH and a boiling point of 64.7°C. It is a versatile compound that is widely used in the production of other chemicals, as well as in the fuel industry.
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Hydrochloric acid is a commonly used laboratory reagent. It is a clear, colorless, and highly corrosive liquid with a pungent odor. Hydrochloric acid is an aqueous solution of hydrogen chloride gas.
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The Folin-Ciocalteu reagent is a colorimetric reagent used for the quantitative determination of phenolic compounds. It is a mixture of phosphomolybdic and phosphotungstic acid complexes that undergo a color change when reduced by phenolic compounds.
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Quercetin is a natural compound found in various plants, including fruits and vegetables. It is a type of flavonoid with antioxidant properties. Quercetin is often used as a reference standard in analytical procedures and research applications.
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Potassium persulfate is an oxidizing agent used in various laboratory and industrial applications. It is a white, crystalline solid that is soluble in water. Potassium persulfate is commonly used as an initiator in free-radical polymerization reactions, as an oxidizing agent, and as a bleaching agent.
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Ethanol is a clear, colorless liquid chemical compound commonly used in laboratory settings. It is a key component in various scientific applications, serving as a solvent, disinfectant, and fuel source. Ethanol has a molecular formula of C2H6O and a range of industrial and research uses.

More about "Potassium carbonate"

Potassium carbonate, also known as K2CO3 or pearl ash, is a versatile chemical compound with a wide range of industrial and commercial applications.
As a crystalline white salt, it is a key ingredient in the production of glass, ceramics, and fertilizers, as well as in the manufacture of soap, detergents, and pharmaceuticals.
One of the primary properties of potassium carbonate is its ability to act as a pH regulator, buffer, and desiccant, making it a valuable component in numerous processes.
Researchers and scientists continue to explore the diverse applications and optimize the efficacy of this essential chemical through rigorous experimentation and analysis.
In addition to its primary uses, potassium carbonate is often compared to related compounds like sodium carbonate (Na2CO3), which is also commonly used in industrial and commercial applications.
Potassium carbonate can also be used in conjunction with other chemicals, such as Gallic acid, DPPH, sodium hydroxide, methanol, hydrochloric acid, Folin-Ciocalteu reagent, quercetin, and potassium persulfate, to achieve specific results in various contexts, including scientific research and product development.
The versatility and importance of potassium carbonate are underscored by the ongoing efforts to optimize its use and explore new applications.
PubCompare.ai's AI-driven protocol comparison platform can help researchers and scientists identify the most effective products and protocols for their potassium carbonate-related studies, enabling them to stay at the forefront of this dynamic and evolving field.