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Potassium phosphate

Potassium phosphate is an essential mineral compound that plays a crucial role in numerous biological processes.
It is involved in energy production, cell signaling, and maintaining proper electrolyte balance within the body.
Potassium phosphate can be found in a variety of food sources, including dairy products, meats, legumes, and whole grains.
Adequate intake of potassium phosphate is important for maintaining healthy muscle and nerve function, as well as supporting cardiovascular health.
Reserch on optimal potassium phosphate supplementation and utilization in scientific experiements can be facilitated by PubCompare.ai, an AI-driven platform that helps locate the most effective protocols from literature, preprints, and patents, ensuring reproducibility and acuracy.
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Most cited protocols related to «Potassium phosphate»

Ultrastructural Analysis of Sciatic Nerve, Spinal Cord, and Muscle in TWI Mice

Cited 231 times

Postnatal day 30 (P30) TWI mice and their WT littermates (5 for each experimental group processed in 5 different experimental sessions, every TWI with its WT littermate) and one P15 TWI mouse versus its WT littermate were perfused with a fixative solution (4% paraformaldehyde and 0.1%–1%–2.5% glutaraldehyde in phosphate buffer, pH 7.4). Sciatic nerves, spinal cords and gastrocnemius muscles were dissected and post-fixed for 4 hours at room temperature in the same fixative solution.
Spinal cords were dissected in the lumbar region, isolating four 1-mm-thick sections in the lumbar enlargement region and the gastrocnemius muscles were cut in small portions, approximately 1 mm³ in volume. Sciatic nerves were processed without further sectioning.
The selected tissues were further treated for epoxy resin embedding as previously described⁴³. Briefly, the samples were deeper fixed in 2–2.5% glutaraldehyde in cacodylate buffer (0.1 M, pH 7.4). After rinsing, specimens were post-fixed with osmium tetroxide (1%)-potassium ferricyanide (1%) in cacodylate buffer, rinsed again, en bloc stained with 3% uranyl acetate in ethanol, dehydrated and embedded in epoxy resin, that was baked for 48 h at 60 °C. Thin sections were obtained with an ultramicrotome (UC7, Leica Microsystems, Vienna, Austria) and collected on G300Cu grids (EMS). Finally, sections were examined with a Zeiss LIBRA 120 plus transmission electron microscope equipped with an in-column omega filter.

Cappello V., Marchetti L., Parlanti P., Landi S., Tonazzini I., Cecchini M., Piazza V, & Gemmi M. (2016). Ultrastructural Characterization of the Lower Motor System in a Mouse Model of Krabbe Disease. Scientific Reports, 6, 1.

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Publication 2016

Buffers Cacodylate Epoxy Resins Ethanol Fixatives Glutaral Hypertrophy Lumbar Region Mice, House Microtomy Muscle, Gastrocnemius Osmium Tetroxide paraform Phosphates potassium ferricyanide Sciatic Nerve Spinal Cord Tissues Transmission Electron Microscopy Ultramicrotomy uranyl acetate

Comprehensive Antioxidant and Enzyme Inhibitory Assays

Cited 78 times

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.

Uysal S., Zengin G., Locatelli M., Bahadori M.B., Mocan A., Bellagamba G., De Luca E., Mollica A, & Aktumsek A. (2017). Cytotoxic and Enzyme Inhibitory Potential of Two Potentilla species (P. speciosa L. and P. reptans Willd.) and Their Chemical Composition. Frontiers in Pharmacology, 8, 290.

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Publication 2017

Engineered ArnA Mutations Optimize Protein Expression

Cited 61 times

Wild type arnA was PCR amplified from E. coli genomic DNA with NdeI and XhoI restriction site overhangs on the 5’ and 3’ ends, respectively, using primers 1F and 1R (See all primer details in Table S1), and cloned into the bacterial expression vector pColaDuet (EMD Millipore). Two serine point mutations were introduced at site 1 (H359S and H361S) using primers 2F and 2R. Two additional serine point mutations were introduced at site 2 (H592S and H593S) using primers 3F and 3R to generate the final arnA mutant containing a total of four histidine to serine mutations.
The arnA knockout strain was generated with the E. coli recombineering technique^{10 (link)}, using the pKD4 plasmid as a template for the selectable marker and BL21(DE3) as the parental strain. The forward and reverse primers, 4F and 4R, were designed to maintain the reading frame of arnB, which shares its start codon with the stop codon of arnA within the arn operon^{11 (link)} (also called pmrHFIJKLM operon^{12 (link)}). A slightly modified scheme was used to introduce the arnA mutant back into the arnA knockout strain at the original locus (Fig. S1). First, mutant arnA was amplified and combined with the amplified selectable marker in a second PCR step. The resulting PCR product containing mutated arnA and the selectable marker was transformed into the arnA knockout strain for recombination using the λ Red recombinase plasmid (pKD46). The selectable marker was eliminated using the FLP plasmid (pCP20). For the modification in slyD, the arnA mutant strain was transformed with a PCR product (generated using primers 5F and 5R) containing a selectable marker flanked by homologous overhangs that, after recombination, result in the elimination of the 46-residue C-terminal, histidine-rich segment of SlyD. Again, the selectable marker was later removed using pCP20. Proper genomic integration was confirmed by PCR and sequencing. The RIL plasmid (Agilent Technologies) encoding rare tRNAs was transformed into the final expression strain to improve the expression of our eukaryotic target proteins.
The binding affinity of wild type and mutant ArnA were assessed by immobilizing purified protein onto a 1 ml His-Trap FF column (GE Healthcare) equilibrated in 50 mM potassium phosphate pH 8.0, 300 mM NaCl, and 5 mM beta-mercaptoethanol. Protein was eluted with a linear gradient of 0–150 mM imidazole. The imidazole concentration at the elution peak of each protein was recorded and compared.
Growth analysis was performed at 18, 25 and 37°C for both LOBSTR and the BL21(DE3) strains carrying the same test expression plasmid (See table S2 for a list of all test constructs). Cultures of 1L were grown in LB medium supplemented with 0.4% (w/v) glucose and antibiotic selection at 37°C to OD600 ~0.7. Protein expression was induced with 0.2 mM IPTG 20 minutes after the cultures were shifted to the desired expression temperature. OD600 was measured from the initial synchronization time and until the cells were harvested ~20–22 hours after induction.
To test protein purification, BL21(DE3) and LOBSTR cultures were started at 37°C in LB medium supplemented with 0.4% (w/v) glucose and appropriate antibiotic selection. At OD600 ~0.7, cultures were shifted to 18°C and induced with 0.2 mM IPTG ~20 min later. Cultures were harvested after 18–20 hours. For each strain and construct tested, a total of ~3.5g of cells were resuspended in 50 mL of resuspension buffer (40 mM potassium phosphate pH 8.0, 150 mM NaCl, 40 mM imidazole, and 3mM beta-mercaptoethanol) and lysed with a cell disrupter (Constant Systems). Lysates were cleared for 25 min at 9500×g and the soluble fraction was incubated with 400 µl bed volume of Ni Sepharose 6 Fast Flow (GE Healthcare) resin for 1 hour while stirring at 4°C. The resin was collected and washed with 6 mL of resuspension buffer and eluted with 2 mL of elution buffer (40 mM potassium phosphate pH 8.0, 150 mM NaCl, 250 mM imidazole, and 3 mM beta-mercaptoethanol). Elution fractions were analyzed on a 4–15 % SDS-PAGE gradient gel (Bio-RAD) and stained with Coomassie Blue R250. Purifications using Ni-NTA (Qiagen) and Talon (Clontech) resins were performed using resuspension buffer containing 20 mM or 5 mM imidazole, respectively, following manufacturer’s recommendations.

Andersen K.R., Leksa N.C, & Schwartz T.U. (2013). Optimized E. coli expression strain LOBSTR eliminates common contaminants from His-tag purification. Proteins, 81(11), 1857-1861.

Publication 2013

2-Mercaptoethanol Antibiotics Autosomal Recessive Polycystic Kidney Disease Bacteria Buffers Cells Claw Cloning Vectors Codon, Initiator Coomassie blue Escherichia coli Eukaryotic Cells Genome Glucose Histidine imidazole Isopropyl Thiogalactoside Mutation Oligonucleotide Primers Parent Plasmids Point Mutation potassium phosphate Proteins Protein Targeting, Cellular Reading Frames Recombinase Recombination, Genetic Resins, Plant SDS-PAGE Sepharose Serine Sodium Chloride Strains Transfer RNA

Deuterium Labeling of Peptides and Proteins

Cited 58 times

Highly deuterated peptides (Waters MassPREP Peptide Standard containing RASG-1, bradykinin, and angiotensin I and II) were prepared by dissolving the lyophilized peptides into D₂O that was adjusted to pD 2.5 with DCl. Peptides were allowed to deuterate at 20 °C for two hours before infusion directly into the instrument in 50:50 D₂O:acetonitrile using a syringe pump.
Labeled cytochrome c (462 µM stock solution in 20 mM Tris, 100 mM NaCl and 3 mM DTT) was diluted to usable concentrations of 64 and 12.8 µM for HPLC and UPLC, respectively. Deuterium exchange was initiated by adding a 15-fold excess of 99% deuterium oxide buffer (20 mM Tris, 100 mM NaCl and 3 mM DTT) at 21 °C. At each exchange-in time point an aliquot (100 picomoles for HPLC, 20 picomoles for UPLC) from the exchange reaction was transferred to a separate tube containing an equal volume of quench buffer (300 mM potassium phosphate, pH 2.6, H₂O). Quenched samples were immediately analyzed. Highly deuterated cytochrome c was prepared by diluting the stock solution 15-fold into D₂O pD 2.5, incubating at 37 °C for 6 hours and quenching as described above.

Wales T.E., Fadgen K.E., Gerhardt G.C, & Engen J.R. (2008). High-speed and high-resolution UPLC separation at zero degrees Celsius. Analytical chemistry, 80(17), 6815-6820.

Publication 2008

acetonitrile Angiotensin I Bradykinin Buffers Cytochromes c Deuterium Deuterium Oxide High-Performance Liquid Chromatographies Peptides potassium phosphate Sodium Chloride Syringes Tromethamine

Isolating White Blood Cells from Whole Blood

Cited 38 times

To generate white blood cells (WBC), red blood cells were lysed from whole human blood, which was collected using either ethylenediaminetetraacetic acid (EDTA) or acid citrate dextrose (ACD) as a coagulant. Blood was mixed at a 1:10 ratio with ammonium-chloride‑potassium (ACK) lysis buffer (150 mM NH₄Cl, 10 mM KHCO₃, 0.1 mM Na₂EDTA, pH 7.4) and incubated for 5 min at room temperature. The WBCs were pelleted by centrifugation (500 ×g, 5 min) at room temperature and then washed with cold phosphate-buffered saline (PBS). For the isolation of human neutrophils, whole blood was mixed with hetasep (Stemcell) in a 1:5 ratio and incubated for 30 min to separate leukocytes from erythrocytes. Subsequently, the straw-colored layer of leukocytes was transferred to a fresh tube and neutrophils were isolated using the direct human neutrophil isolation kit (Stemcell) according to manufacturer's instructions. Both WBCs and purified neutrophils were finally diluted in complete R10 media (RPMI-1640 media (Sigma) with 10% FBS, 2 mM L-Gluthamine and 100 U/ml penicillin/streptomycin) for each assay.

Karsten C.B., Mehta N., Shin S.A., Diefenbach T.J., Slein M.D., Karpinski W., Irvine E.B., Broge T., Suscovich T.J, & Alter G. (2019). A versatile high-throughput assay to characterize antibody-mediated neutrophil phagocytosis. Journal of Immunological Methods, 471, 46-56.

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Publication 2019

acid citrate dextrose Ammonium Biological Assay Blood Centrifugation Chloride, Ammonium Coagulants Cold Temperature Edetic Acid Erythrocytes Homo sapiens isolation Leukocytes Neutrophil Penicillins Phosphates Potassium potassium bicarbonate Potassium Chloride Saline Solution Stem Cells Streptomycin

Most recents protocols related to «Potassium phosphate»

Potassium and Phosphate Solubilization Assay

Not available on PMC !

The isolation of bacteria with the K solubilization test aims to determine bacteria that can dissolve potassium (K). The media used is Alexandrov media with point inoculation and incubation for 1 week or 7 days at room temperature (Safriani et al., 2020) . Bacteria can be categorized as potassium solvents if they produce a clear zone around the isolate. The potassium solubilization index is measured based on the SI (Solubilization Index) formula, SI = 𝑋𝐼-𝑋2 𝑋2 , with XI = clear zone diameter and X2 = colony zone diameter (Lau et al., 2020) (link).
Qorisha Lutfia Prameselly, et al. / Biosaintifika 16 (1) (2024): [181] [182] [183] [184] [185] [186] [187] [188] [189] [190] The P solvent test was conducted to determine the bacteria capable of dissolving phosphate. The media used in this test is Pikovskaya media (PK) with point inoculation and incubation for 6-7 days at room temperature (Safriani et al., 2020; Putri et al., 2020) . Bacteria are considered to have the ability to solubilize phosphate if they can produce a clear zone around the isolate. The index used to calculate the ability of bacteria to dissolve phosphate is the formula, SI = 𝑋𝐼-𝑋2 𝑋2 .

Prameselly Q.L., Sugiharto B., & Fatmawati U. (2024). Characterization of Chitinolitic Bacteria from Hermatia illucent Larvae Waste: Antifungal Activity, Hydrolytic Enzyme, and Phosphate-Potassium Solubilization. Biosaintifika Journal of Biology & Biology Education, 15(1), 181-190.

Publication 2024

Phosphate and Potassium Solubilization Assay

The following assays were conducted with slight modifications (Cui et al., 2019 (link)) to assess specific traits: The phosphate-solubilizing capability of BA-4 was assessed using Pikovskaya (PVK) agar medium (10 g glucose, 5 g Ca₃(PO₄)₂, 0.2 g NaCl, 0.5 g (NH₄)2SO₄, 0.1 g MgSO₄·7H₂O, 0.2 g KCl, 0.5 g yeast extract, 2 mg MnSO₄, 2 mg FeSO₄·7H₂O, 25 mg Bromphenol blue, 15 g agar in 1L, pH 7.2). A bacterial cell suspension of BA-4 (10 μL) was inoculated onto PVK plates and incubated at 28°C for 7 days to evaluate its ability to utilize inorganic phosphate from Ca₃(PO₄)₂ as the sole phosphate source. Similarly, the potassium-solubilizing capability of BA-4 was determined on potassium feldspar (PF) agar medium (10 g sucrose, 0.5 g MgSO₄·7H₂O, 0.2 g (NH₄)₂SO₄, 0.1 g NaCl, 0.1 g CaCO₃, 5.0 g Potassium feldspar, 25 mg Bromophenol blue, 15 g agar in 1 L, pH 7.2). The appearance of a clear zone around the bacterial colony after 7 days at 28°C were considered positive for its ability to solubilize Phosphate and potassium.

Li B., He X., Guo S., Li D., Wang Y., Meng X., Dai P., Hu T., Cao K, & Wang S. (2024). Characterization of Bacillus amyloliquefaciens BA-4 and its biocontrol potential against Fusarium-related apple replant disease. Frontiers in Plant Science, 15, 1370440.

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Publication 2024

Phosphate and Potassium Solubilization Assays

We conducted the phosphate solubilizing activity using NBRIY broth, supplemented with 5 g l⁻¹ tricalcium phosphate or Moroccan phosphate rock as the exclusive inorganic phosphate source (Nafis et al. 2019 ). The medium was inoculated with a 200-µl yeast solution, washed three times with PW, and adjusted to an optical density (OD₆₀₀) of 0.1. The medium was then incubated at 28°C on a rotatory shaker, agitating at 140 rpm, for 96 h. After incubation, the yeast cells were separated by centrifugation (6000 rpm) for 10 min. In the supernatant, we measured the pH and soluble phosphate as described by Nagul et al. (2015 (link)).
Potassium solubilization capacity was determined onto Aleksandrov agar medium supplemented with 5 g l⁻¹ Mica powder (Meena et al. 2015 ). The agar plates were inoculated following the drop-on-plate method described by Alikhani et al. (2006 ) with a bacterial solution washed and adjusted to OD₆₀₀ = 0.8. The plates were incubated for 7 days at 30°C, and the results were displayed as the ratio of the clear zone surrounding the colonies and the diameter of the colony.

Raklami A., Babalola O.O., Jemo M, & Nafis A. (2024). Unlocking the plant growth-promoting potential of yeast spp.: exploring species from the Moroccan extremophilic environment for enhanced plant growth and sustainable farming. FEMS Microbiology Letters, 371, fnae015.

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Publication 2024

Phosphate Buffer Solution Preparation

Not available on PMC !

Solution A was prepared by using potassium mono hydrogen phosphate 250 mM and solution B was prepared by taking potassium dimono hydrogen phosphate 250 mM. Both the solutions were mixed and pH was set at 7.8. Methionine was prepared by taking 100 mM in 10 ml distilled water. Riboflavin was prepared by taking 10 mM in 10ml distilled water, EDTA was made by taking 5 mM in 10 ml distilled water and nitroblue tetrazolium (NBT) was prepared by taking 750 µM in 300 µl distilled water.

- P.K., Vishnuvardhan.Z, & K. B. (2024). A Hydroponic Approach to Evaluate Morpho-physiological and Biochemical Responses of Kodo Millet (Paspalum Scrobiculatum) Genotypes Against Calcium Chloride Stress. International Journal For Multidisciplinary Research, 6(2).

Publication 2024

Quantitative Evaluation of Nutrient Solubilization

Potassium solubilization by the selected strains was quantitatively measured using Aleksandrov broth. The bacterial isolates were introduced into a 40 ml volume of Aleksandrov broth and subjected to incubation in a rotary shaker operating at 4.26 g for a duration of 5 days at a temperature of 30°C. As a control, broth was autoclaved. After incubation, pH of the broth was noted. Post incubation, the broth was centrifuged at a speed of 42,600 × g for 10 min. The supernatant was collected and then utilized for the purpose of measuring the concentration of soluble potassium using a flame photometer. Various concentrations (20, 30, and 40 mg L⁻¹) of potassium chloride solution were prepared as standard solutions for the measurement of present K levels (Rajawat et al., 2016 (link)).
The potential of Zn solubilization by the isolated bacteria was quantitatively checked by following the protocol proposed by Fasim et al. (2002 (link)). Overnight grown bacterial cultures (2.5% inoculum) were inoculated in tris minimal salts medium (250 ml) supplied with 14 mM zinc oxide and non-supplemented medium was used as a control without inoculation. Bacterial strains were kept on orbital shaker to incubate for 10 days at 30°C. The pH of samples was measured every day. The medium was centrifuged and the supernatants were collected. The supernatants were acidified using 6 M HNO₃ and the soluble ZN content was measured by atomic absorption spectrophotometry (AAS). The solubilized zinc content was determined by measuring the difference between the soluble zinc in the inoculation sample and the equivalent control and expressing it as grams of Zn ml⁻¹ culture.
National botanical research institute's phosphate (NBRIP) medium was utilized to quantitatively measure the phosphate solubilizing ability of isolated bacteria (Nautiyal, 1999 (link)). The cultures were grown for 24 h and then 1 ml culture was inoculated into 50 ml NBRIP medium. The medium was put in an incubator at 17.04 × g for 6 days at 28±2°C in an orbital shaking incubator. The pH of the medium was recorded and uninoculated medium taken as a control. Post incubation, the cultures were subjected to centrifuge at 27,264 × g for 20 min and supernatants were obtained. Available phosphate in the culture supernatants were quantified by following the vanadomolybdophosphoric acid colorimetric method (Kumar et al., 2009 (link)).

Patel M., Islam S., Glick B.R., Choudhary N., Yadav V.K., Bagatharia S., Sahoo D.K, & Patel A. (2024). Zero budget natural farming components Jeevamrit and Beejamrit augment Spinacia oleracea L. (spinach) growth by ameliorating the negative impacts of the salt and drought stress. Frontiers in Microbiology, 15, 1326390.

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Publication 2024

Top products related to «Potassium phosphate»

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Acetonitrile by Merck Group

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Acetonitrile is a colorless, volatile, flammable liquid. It is a commonly used solvent in various analytical and chemical applications, including liquid chromatography, gas chromatography, and other laboratory procedures. Acetonitrile is known for its high polarity and ability to dissolve a wide range of organic compounds.

Bovine serum albumin (bsa) by Merck Group

Sourced in United States, Germany, United Kingdom, China, Italy, Japan, France, Sao Tome and Principe, Canada, Macao, Spain, Switzerland, Australia, India, Israel, Belgium, Poland, Sweden, Denmark, Ireland, Hungary, Netherlands, Czechia, Brazil, Austria, Singapore, Portugal, Panama, Chile, Senegal, Morocco, Slovenia, New Zealand, Finland, Thailand, Uruguay, Argentina, Saudi Arabia, Romania, Greece, Mexico

Bovine serum albumin (BSA) is a common laboratory reagent derived from bovine blood plasma. It is a protein that serves as a stabilizer and blocking agent in various biochemical and immunological applications. BSA is widely used to maintain the activity and solubility of enzymes, proteins, and other biomolecules in experimental settings.

Gallic acid by Merck Group

Sourced in United States, Germany, Italy, Spain, France, India, China, Poland, Australia, United Kingdom, Sao Tome and Principe, Brazil, Chile, Ireland, Canada, Singapore, Switzerland, Malaysia, Portugal, Mexico, Hungary, New Zealand, Belgium, Czechia, Macao, Hong Kong, Sweden, Argentina, Cameroon, Japan, Slovakia, Serbia

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.

Ethanol by Merck Group

Sourced in Germany, United States, United Kingdom, Italy, India, France, China, Australia, Spain, Canada, Switzerland, Japan, Brazil, Poland, Sao Tome and Principe, Singapore, Chile, Malaysia, Belgium, Macao, Mexico, Ireland, Sweden, Indonesia, Pakistan, Romania, Czechia, Denmark, Hungary, Egypt, Israel, Portugal, Taiwan, Province of China, Austria, Thailand

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.

What are the main uses and benefits of Potassium phosphate?

Potassium phosphate is an essential mineral compound that plays a crucial role in numerous biological processes. It is involved in energy production, cell signaling, and maintaining proper electrolyte balance within the body. Adequate intake of potassium phosphate is important for maintaining healthy muscle and nerve function, as well as supporting cardiovascular health.

What are some common food sources of Potassium phosphate?

How can PubCompare.ai help with Potassium phosphate research?

PubCompare.ai allows you to screen protocol literature more efficiently and leverage AI to pinpoint critical insights. The platform can help researchers identify the most effective protocols related to Potassium phosphate for their specific research goals. PubComapre.ai's AI-driven analysis can highlight key differences in protocol effectiveness, enabling you to choose the best option for reproducibility and accuracy.

Are there any common challenges or considerations when using Potassium phosphate?

One potential challenge with using Potassium phosphate is ensuring proper dosage and electrolyte balance. Too much or too little Potassium phosphate can have adverse effects, so it's important to follow recommended guidelines and consult with a healthcare professional, especially when using supplements. PubCompare.ai can help researchers identify the optimal Potassium phosphate protocols and products to avoid these issues.

What are the different forms or variations of Potassium phosphate?

Potassium phosphate comes in several different chemical forms, including monobasic potassium phosphate (KH2PO4), dibasic potassium phosphate (K2HPO4), and tribasic potassium phosphate (K3PO4). These variations can have slightly different properties and uses, so it's important to select the appropriate form for your specific application or research needs. PubCompare.ai can help you compare the efficacy and characteristics of different Potassium phosphate products.

More about "Potassium phosphate"

dipotassium phosphate, monopotassium phosphate, K+, PO4^3-, potassium ions, phosphate ions, muscle cramps, fatigue, cardiac arrhythmias, sodium chloride, sodium hydroxide, potassium dihydrogen phosphate, hydrochloric acid, potassium chloride, methanol, acetonitrile, bovine serum albumin, gallic acid, ethanol