Log In Sign up
The largest database of trusted experimental protocols
> Chemicals & Drugs > Amino Acid > Potassium Glutamate

Potassium Glutamate

Potassium glutamate is a salt of the amino acid glutamic acid and the mineral potassium.
It is commonly used as a food additive to enhance savory flavors.
Potassium glutamate has been studied for its potential therapeutic applications, such as its role in supporting cognitive function and reducing fatigue.
Researhcers can use PubCompare.ai to quickly identify the most effective potassium glutamate protocols from the scientific literature, pre-prints, and patents to streamline their research and optimize their studies.

Most cited protocols related to «Potassium Glutamate»

1
Cell-Free Protein Synthesis Protocol
The CFPS reactions were carried out in a 1.5 mL microtube in the incubator. The standard reaction mixture for CFPS consists of the following components in a final volume of 15 μL: 1.2 mM ATP; 0.85 mM each of GTP, UTP, and CTP; 34.0 μg mL−1 L-5-formyl-5, 6, 7, 8-tetrahydrofolic acid (folinic acid); 170.0 μg mL−1 of E. coli tRNA mixture; 130 mM potassium glutamate; 10 mM ammonium glutamate; 12 mM magnesium glutamate; 2 mM each of 20 amino acids; 10 μM of L-[14C(U)]-leucine (11.1 GBq mmol−1, PerkinElmer, Waltham, MA); 0.33 mM nicotinamide adenine dinucleotide (NAD); 0.27 mM coenzyme-A (CoA); 1.5 mM spermidine; 1 mM putrescine; 4 mM sodium oxalate; 33 mM phosphoenolpyruvate (PEP); 13.3 μg mL−1 plasmid; 100 μg mL−1 T7 RNA polymerase, and 27% v/v of cell extract. The CFPS reactions were carried out at 37°C for 4 hours.
Kwon Y.C, & Jewett M.C. (2015). High-throughput preparation methods of crude extract for robust cell-free protein synthesis. Scientific Reports, 5, 8663.
Full text: Click here
Publication 2015
5,6,7,8-tetrahydrofolic acid Amino Acids Ammonium bacteriophage T7 RNA polymerase Cell Extracts CFP protocol Coenzyme A Coenzyme I Escherichia coli Glutamates Leucine Leucovorin Magnesium Phosphoenolpyruvate Plasmids Potassium Glutamate Putrescine Sodium Oxalate Spermidine Transfer RNA
2
Generating B. subtilis Mutants via Natural Competence

Protocol full text hidden due to copyright restrictions

Open the protocol to access the free full text link

Publication 2017
Agar Antibiotics casamino acids Cells Erythromycin ferric ammonium citrate Glucose Glycerin Kanamycin Lincomycin manganese chloride Potassium Aspartate Potassium Glutamate potassium phosphate, dibasic Sodium Citrate Dihydrate Sulfate, Magnesium Tryptophan Yeast, Dried
3
Spectrophotometric Assay of RecA-Mediated dATP Hydrolysis
The ssDNA-dependent dATP hydrolysis activity of RecA protein was observed via a coupled spectrophotometric enzyme assay (38 (link),39 (link)). Absorbance measurements were taken with a Shimadzu CPS-240A dual-beam spectrophotometer equipped with a temperature controller and 6-position cell chamber. The cell path length and band pass were 1 cm and 2 nm, respectively. The regeneration of dATP from dADP and phosphoenolpyruvate driven by the oxidation of NADH can be followed by a decrease in absorbance at 340 nm. Rates of ssDNA-dependent RecA-mediated dATP hydrolysis and the lag times were measured in buffer D (50 mM Tris–HCl, pH 7.5, 1 mM DTT, 90 mM NaCl, 10 mM MgOAc, 50 µg/ml BSA, 5% glycerol) containing 5 mM dATP for variable time at 37°C in a 100-µl reaction mixture. A dATP regeneration system (0.5 mM phosphoenolpyruvate, 10 U/ml pyruvate kinase) and a coupling system (0.25 mM NADH, 10 U/ml lactate dehydrogenase, 3 mM potassium glutamate) were also included. The orders of addition of 3199-nt pGEM ssDNA (10 µM in nt), the proteins and their concentrations were indicated in the text. The amount of dADP was calculated as describe (40 (link)).
Yadav T., Carrasco B., Myers A.R., George N.P., Keck J.L, & Alonso J.C. (2012). Genetic recombination in Bacillus subtilis: a division of labor between two single-strand DNA-binding proteins. Nucleic Acids Research, 40(12), 5546-5559.
Publication 2012
Buffers Cells DNA, Single-Stranded Enzyme Assays Glycerin Hydrolysis Lactate Dehydrogenase NADH Phosphoenolpyruvate Potassium Glutamate prostaglandin M Proteins Pyruvate Kinase Rec A Recombinases Regeneration Sodium Chloride Spectrophotometry Tromethamine
4
Cell-Free Protein Synthesis Protocol
The PCR-generated DNA template was expressed in a cell-free transcription-translation system (PURExpress In Vitro Protein Synthesis kit, New England BioLabs) (11 (link)). For a typical reaction, 2 µl of solution A (kit), 1 µl of solution B (kit), 0.5 µl of DNA template (0.2 pmol/µl), 0.5 µl of radioactive primer (1 pmol), 0.2 µl of Ribolock RNAse inhibitor (40 U/µl, Thermo Scientific), 0.5 µl of the compound to be tested (10X solution in H2O) and 0.3 µl of H2O were combined in the reaction tube chilled on ice. Samples were incubated at 37°C for 20 min.
For the reactions that were run at a reduced concentration of amino acids, a modified solution A (11 (link)) was prepared to contain 125 mM Hepes-KOH (pH 7.6), 250 mM potassium glutamate, 15 mM magnesium acetate, 5 mM spermidine, 2.5 mM DTT, 25 µg/ml formyl donor (see later in the text), 50 mM creatine phosphate (Sigma), 5 mg/ml Escherichia coli tRNA (Roche), 15 µM each amino acid, 5 mM ATP, 5 mM GTP, 2.5 mM CTP, 2.5 mM UTP (pH of all the nucleotide triphosphate stocks was previously adjusted to 7.5). The formyl donor solution was prepared by dissolving 25 mg of calcium folinic acid (Sigma) in 2 ml of 50 mM 2-mercaptoethanol, adding 220 µl of 12 N HCl and incubating the reaction at room temperature for 3 h. The solution was diluted to 1 mg/ml with H2O and stored in 100 µl of aliquots at −20°C.
Orelle C., Szal T., Klepacki D., Shaw K.J., Vázquez-Laslop N, & Mankin A.S. (2013). Identifying the targets of aminoacyl-tRNA synthetase inhibitors by primer extension inhibition. Nucleic Acids Research, 41(14), e144.
Publication 2013
2-Mercaptoethanol Amino Acids Cell-Free System Escherichia coli HEPES Leucovorin, Calcium magnesium acetate Nucleotides Oligonucleotide Primers Phosphocreatine Potassium Glutamate Protein Biosynthesis Radioactivity RNase 2 Spermidine Tissue Donors Transcription, Genetic Transfer RNA triphosphate
5
Reconstitution of DNA Helicase Loading Complex

Protocol full text hidden due to copyright restrictions

Open the protocol to access the free full text link

Publication 2014
adenosine 5'-O-(3-thiotriphosphate) Buffers Creatine Kinase Deoxyribonuclease I Dithiothreitol DNA Helicase A DNA Helicases Edetic Acid Egtazic Acid Glycerin HEPES HSP40 Heat-Shock Proteins Krypton magnesium acetate MCM2 protein, human Phosphocreatine Potassium Glutamate Proteins SDS-PAGE Sodium Chloride Stains Staphylococcal Protein A Zinc Acetate

Most recents protocols related to «Potassium Glutamate»

1
High-Throughput Screening Assay for DnaE1
For the high-throughput
screening assays, we used the same oligonucleotides used for the manual
assays (see Table S1). The oligonucleotides
and protein (M. tuberculosis DnaE1)
were diluted in 50 mM HEPES pH 7.5, 100 mM potassium glutamate, and
0.5 mg/mL BSA. Assays were dispensed using a Mantis liquid handler
(Formulatrix) in 384-well polypropylene plates from Corning #4514.
Data were collected for 30 cycles, each lasting for 60 s.
The
assay validation statistics (Figure S4)
were calculated using the following formulas: where the mean signal is the fluorescent signal
at completion of the assay in the presence of DNA and protein. The
mean background is the negative control, where only DNA was added. where “SD of sample” is the
standard deviation of the positive control (DNA + protein) and the
“SD of control” is the standard deviation of the negative
control (DNA only).
Botto M.M., Murthy S, & Lamers M.H. (2023). High-Throughput Exonuclease Assay Based on the Fluorescent Base Analogue 2-Aminopurine. ACS Omega, 8(9), 8285-8292.
Publication 2023
Biological Assay Diet, Formula HEPES Mycobacterium tuberculosis Oligonucleotides Polypropylenes Potassium Glutamate Proteins
2
Fluorescence-based Enzymatic Activity Assay
Assays were performed
using oligonucleotides in Table S1. Fluorescence
emission data were collected using a PHERAstar FSX microplate reader.
All of the substrates and the proteins were individually diluted in
50 mM HEPES pH 7.5, 100 mM potassium glutamate, 5 mM MgCl2, and 0.5 mg/mL BSA unless otherwise stated. Reactions were started
by adding protein to DNA in a Corning 384-well Low Volume Black Round
Bottom Polystyrene NBS Microplate (Corning #4514). Data were collected
for 50 cycles, each lasting 20 s. All of the steps were performed
at room temperature.
The samples were excited at 330 nm, and
the emission was collected at 380 nm (for excitation and emission
spectra, see Figure S3). A 320–380
filter (1904A1 BMG Labtech) was used to collect the measurements.
To be able to compare measurements taken on different days with different
exonucleases and on different substrates, all assays were performed
using the same gain.
Botto M.M., Murthy S, & Lamers M.H. (2023). High-Throughput Exonuclease Assay Based on the Fluorescent Base Analogue 2-Aminopurine. ACS Omega, 8(9), 8285-8292.
Publication 2023
Biological Assay HEPES HSP40 Heat-Shock Proteins Magnesium Chloride Oligonucleotides Polystyrenes Potassium Glutamate Proteins
3
RisR Binding to Radiolabeled Promoters
Plasmids pPK14640 and pPK14641 were isolated using a QIAfilter maxi kit (Qiagen), and 30 ng was digested using BamHI and HindIII enzymes (NEB) to expose the 3′ ends of the fragment for radiolabeling with [α-32P]dGTP (PerkinElmer) by Sequenase (Thermo Fisher). The relevant fragments were separated and isolated from a 5% acrylamide-TBE (Tris-borate-EDTA) gel using a QIAquick gel extraction kit (Qiagen). Promoter fragments were incubated with RisR (1 μM) for 25 min in 25 mM potassium phosphate buffer, 30 mM KCl, 5 mM potassium glutamate, 100 μg/mL BSA, and 1 mM DTT at 37°C under anaerobic conditions. DNase I (Worthington) 2 μg/mL in 65 mM MgCl2 was added for 30 s, and the reaction was terminated with 300 mM acetate and 20 mM EDTA, ethanol precipitated and resuspended in 4 μL urea loading dye, heated to 90°C for 1 min before loading a 7-M urea −8.0% polyacrylamide gel in 0.5× TBE buffer. The G+A ladder for each radiolabeled promoter fragment was achieved by DNA modification using formic acid followed by piperidine cleavage (79 (link)). The gel was visualized in an Amersham Typhoon 5-gel imaging scanner (Cytiva). For some experiments, 5 μM RisR was treated with 32 units of enterokinase (NEB) to remove the N-terminal tag by 2 h of incubation at room temperature under anaerobic conditions in 50 mM potassium phosphate buffer, 100 mM NaCl, 2 mM CaCl2, and 10% glycerol pH 7.2.
Sourice M., Askenasy I., Garcia P.S., Denis Y., Brasseur G., Kiley P.J., Py B, & Aubert C. (2023). A Diverged Transcriptional Network for Usage of Two Fe-S Cluster Biogenesis Machineries in the Delta-Proteobacterium Myxococcus xanthus. mBio, 14(1), e03001-22.
Full text: Click here
Publication 2023
Acetate Acrylamide Borates Buffers Cytokinesis deoxyguanosine triphosphate Deoxyribonuclease I Edetic Acid Enteropeptidase Enzymes Ethanol formic acid Glycerin Magnesium Chloride piperidine Plasmids polyacrylamide gels Potassium Glutamate potassium phosphate sequenase Sodium Chloride Tris-borate-EDTA buffer Tromethamine Typhoons Urea
4
In Vivo Glutamate and Potassium Recordings Using MEA-Pipette Assemblies
Amperometric recordings performed here were similar to previously published methods [13 (link), 23 (link), 24 ]. Briefly, a constant voltage was applied to the MEA using the FAST16 mkIII recording system. In vivo recordings were performed at an applied potential of +0.7 V compared to the silver/silver chloride reference electrode wire. All data were recorded at a frequency of 10 Hz and amplified by the headstage piece (2 pA/mV). Immediately prior to implantation of the glutamate-selective MEA-pipette assembly, the pipette was filled with 120 mM of KCl (120 mM KCl, 29 mM NaCl, 2.5 mM CaCl2, pH 7.2 to 7.5) or 100 μM L-glutamate (100 μM L-glutamate in 0.9% sterile saline pH 7.2–7.5) immediately prior to implantation and in vivo recording. The concentrations for both solutions have been previously shown to elicit reproducible potassium-evoked glutamate overflow or exogenous glutamate peaks [15 (link), 25 (link), 26 (link)]. Solutions were filtered through a 0.20 μm sterile syringe filter (Sarstedt AG & Co. Numbrecht, Germany) attached to a 1 mL syringe with a 4-inch, 30-gauge stainless steel needle with a beveled tip (Popper and Son, Inc, NY) while filling the micropipette. The open end of the micropipette end was then connected to a Picospritzer III (Parker-Hannin Corp., General Valve Corporation, OH) with settings to dispense fluid through the use of nitrogen gas in nanoliter quantities as measured by a dissecting microscope (Meiji Techno, San Jose, CA) with a calibrated reticule in the eyepiece [27 (link), 28 ].
Once the MEA-micropipette apparatus was securely attached to the Picospritzer and FAST system, bregma was measured using an ultraprecise stereotaxic arm. MEA-micropipette constructs were implanted in the cortex (AP, −2.8 mm; ML, ±5.0 mm; DV, −1.0 mm vs. bregma), hippocampus (AP, −3.5 mm; ML, ±3.0 mm; DV, −2.6 to −3.75 mm vs. bregma) and thalamus (AP, −3.5 mm; ML, ±3.0 mm; DV, −5.6 mm vs. bregma) based on the coordinates from Paxinos and Watson [29 ] (Figure 3A). Glutamate and KCl-evoked measures were recorded in both hemispheres in a randomized and balanced experimental design to mitigate possible hemispheric variations or effects of anesthesia duration.
Beitchman J.A., Krishna G., Bromberg C.E, & Thomas T.C. (2023). Effects of isoflurane and urethane anesthetics on glutamate neurotransmission in rat brain using in vivo amperometry. bioRxiv.
Full text: Click here
Publication Preprint 2023
Anesthetic Effect Cortex, Cerebral Glutamates Microscopy Needles Nitrogen Normal Saline Ovum Implantation Potassium Glutamate Seahorses silver chloride Sodium Chloride Stainless Steel Strains Syringes Thalamus
5
Cell-free Protein Expression in E. coli
All TxTl experiments were
performed using the E. coli cell extract
prepared, according to the published protocol.26 (link) We used Rosetta 2 (DE3) E. coli strain to prepare all extracts.
For cell extract preparation,
cells were grown in 2xYTPG media at 30 °C to OD of 0.5. For each
TxTl reaction, the final concentration of reagents was from the energy
mix: 500 mM HEPES pH 8, 15 mM ATP and GTP, 9 mM CTP and UTP, 2 mg/mL
of E. coli tRNA mixture, 0.68 mM folinic
acid, 3.3 mM nicotinamide adenine dinucleotide (NAD), 2.6 mM coenzyme-A
(CoA), 15 mM spermidine, 40 mM sodium oxalate, 7.5 mM cAMP, 300 mM
3-PGA; from the amino acid mix: 2 mM each of alanine, arginine, asparagine,
aspartic acid, cysteine, glutamic acid, glutamine, glycine, histidine,
isoleucine, leucine, lysine, methionine, phenylalanine, proline, serine,
threonine, tryptophan, tyrosine and valine; and from the salt mix:
130 mM potassium glutamate, 10 mM ammonium acetate, and 10 mM magnesium
glutamate.27 (link)Due to the batch-to-batch
variability of TxTl preparation yields,
we performed all of the directly comparable experiments (experiments
shown on the same figure) using the same batch of the extract.
Cash B., Gaut N.J., Deich C., Johnson L.L., Engelhart A.E, & Adamala K.P. (2023). Parasites, Infections, and Inoculation in Synthetic Minimal Cells. ACS Omega, 8(7), 7045-7056.
Publication 2023
Alanine Amino Acids ammonium acetate Arginine Asparagine Aspartic Acid Cell Extracts Cells Coenzyme A Coenzyme I Cysteine Escherichia coli Glutamic Acid Glutamine Glycine HEPES Histidine Isoleucine Leucine Lysine Methionine Phenylalanine Potassium Glutamate Proline Serine Sodium Chloride Sodium Oxalate Spermidine Strains Threonine Transfer RNA Tryptophan Tyrosine Valine

Top products related to «Potassium Glutamate»

1
Collagenase type 2 by Worthington
Sourced in United States, United Kingdom, Jersey, Germany, Japan, Switzerland, Canada, Australia, France
Collagenase type II is an enzyme used in cell and tissue culture applications. It is responsible for the breakdown of collagen, a structural protein found in the extracellular matrix. This enzyme is commonly used to facilitate the dissociation of cells from tissues during cell isolation and harvesting procedures.
2
Typhoon 8600 by GE Healthcare
Sourced in United States, United Kingdom
The Typhoon 8600 is a high-performance imager designed for a variety of life science applications. It can capture images of gels, blots, and other samples using multiple detection modes, including fluorescence, chemiluminescence, and phosphor imaging.
3
Imagequant software by GE Healthcare
Sourced in United States, United Kingdom, Sweden, Germany, Austria, Australia
ImageQuant software is a data analysis tool designed for quantitative analysis of digital images. It enables users to capture, process, and analyze images from various laboratory equipment, such as gel imagers and blot imaging systems. The software provides tools for image acquisition, image processing, and data analysis, allowing researchers to quantify and compare signals within their samples.
4
Adenosine triphosphate (atp) by Merck Group
Sourced in United States, Germany, United Kingdom, China, Sao Tome and Principe, Italy, Japan, Macao, Spain, Canada, France, Switzerland, Ireland, Sweden, Australia
ATP is a laboratory instrument used to measure the presence and concentration of adenosine triphosphate (ATP) in various samples. ATP is a key molecule involved in energy transfer within living cells. The ATP product provides a reliable and accurate method for quantifying ATP levels, which is useful in applications such as microbial detection, cell viability assessment, and ATP-based assays.
5
Oxygraph 2k by Oroboros
Sourced in Austria
The Oxygraph-2k is a high-performance respirometer designed for precise measurement of oxygen consumption and production in biological samples. It provides real-time monitoring of oxygen levels, making it a valuable tool for researchers in the fields of cell biology, physiology, and bioenergetics.
6
Cls3694 by Corning
CLS3694 is a piece of lab equipment designed for clinical and laboratory use. It serves as a core function for performing various analytical and testing procedures. The detailed specifications and intended uses of this product are not available within the scope of this response.
7
Creatine kinase by Roche
Sourced in Switzerland, United States, Japan, Germany
Creatine kinase is a laboratory test used to measure the levels of the enzyme creatine kinase in the blood. Creatine kinase is an enzyme that plays a role in providing energy to muscles. It can be used to help diagnose and monitor certain medical conditions, such as muscle damage or disorders.
8
Molecular imager fx by Bio-Rad
Sourced in United States, Germany, China
The Molecular Imager FX is a laboratory instrument designed for the detection and analysis of fluorescent and chemiluminescent samples. It is capable of imaging a wide range of sample types, including gels, blots, and microplates, using a variety of detection methods.
9
Typhoon imager by GE Healthcare
Sourced in United States, United Kingdom
The Typhoon imager is a high-performance fluorescence and luminescence imaging system designed for life science research. It offers sensitive detection and quantification of a wide range of fluorescent and chemiluminescent labels and dyes. The Typhoon imager is capable of scanning various sample formats, including gels, blots, and microplates.
10
Myone by Thermo Fisher Scientific
Sourced in Norway
The MyOne is a magnetic bead-based separation system designed for high-throughput sample preparation. It provides efficient and consistent separation of magnetic particles from liquid samples, enabling automated processing of multiple samples simultaneously. The core function of the MyOne is to facilitate rapid and reliable separation of target analytes from complex matrices using magnetic particle technology.

More about "Potassium Glutamate"

Potassium glutamate, also known as E 622 or potassium monosodium glutamate (E 622), is a salt of the amino acid glutamic acid and the mineral potassium.
It is commonly used as a food additive to enhance savory, umami flavors in a variety of processed foods, such as soups, sauces, and seasonings.
Potassium glutamate has been studied for its potential therapeutic applications, including its role in supporting cognitive function and reducing fatigue.
Researchers can utilize platforms like PubCompare.ai to quickly identify the most effective potassium glutamate protocols from the scientific literature, pre-prints, and patents, helping to streamline their research and optimize their studies.
The use of potassium glutamate as a food additive has been the subject of some controversy, with concerns raised about its potential health effects.
However, numerous studies have found potassium glutamate to be generally safe for consumption when used in moderation.
In addition to its culinary and potential therapeutic uses, potassium glutamate has also been studied for its applications in other areas, such as its role in supporting the growth and development of certain microorganisms.
Researchers may use tools like Collagenase type II, Typhoon 8600, ImageQuant software, ATP, Oxygraph-2k, CLS3694, Creatine kinase, Molecular Imager FX, Typhoon imager, and MyOne to investigate these various applications of potassium glutamate.
Overall, potassium glutamate is a versatile and widely-used compound with a range of potential applications, both in the food industry and in the realm of scientific research.
By staying up-to-date with the latest research and utilizing powerful tools like PubCompare.ai, researchers can continue to explore the full potential of this fascinating compound.