> Chemicals & Drugs > Amino Acid > Glutamine

Glutamine

Glutamine is a nonessential amino acid that plays a crucial role in various metabolic processes within the human body.
It serves as a precursor for the synthesis of other amino acids, proteins, and nucleic acids, and is also involved in energy production, acid-base balance, and immune function.
Glutamine is particularly important for the health and function of the gastrointestinal tract, muscle tissue, and the brain.
Adequate glutamine levels are essential for maintaining overall wellbeing and supporting the body's natural healing and repair processes.
Researchers continue to explore the potential therapeutic applications of glutamine supplementation in a wide range of clinical conditions, including sports performance, critical illness, and neurological disorders.
This MeSH term provides a concise, informative overview of the physiological importance and research areas related to glutamine.

Most cited protocols related to «Glutamine»

Quantitative Proteomics of HeLa-E. coli Mixture

Cited 284 times

An Escherichia coli K12 strain was grown in standard LB medium, harvested, washed in PBS, and lysed in BugBuster (Novagen Merck Chemicals, Schwalbach, Germany) according to the manufacturer's protocol. HeLa S3 cells were grown in standard RPMI 1640 medium supplemented with glutamine, antibiotics, and 10% FBS. After being washed with PBS, cells were lysed in cold modified RIPA buffer (50 mm Tris-HCl, pH 7.5, 1 mm EDTA, 150 mm NaCl, 1% N-octylglycoside, 0.1% sodium deoxycholate, complete protease inhibitor mixture (Roche)) and incubated for 15 min on ice. Lysates were cleared by centrifugation, and after precipitation with chloroform/methanol, proteins were resuspended in 6 m urea, 2 m thiourea, 10 mm HEPES, pH 8.0. Prior to in-solution digestion, 60-μg protein samples from HeLa S3 lysates were spiked with either 10 μg or 30 μg of E. coli K12 lysates based on protein amount (Bradford assay). Both batches were reduced with dithiothreitol and alkylated with iodoacetamide. Proteins were digested with LysC (Wako Chemicals, GmbH, Neuss, Germany) for 4 h and then trypsin digested overnight (Promega, GmbH, Mannheim, Germany). Digestion was stopped by the addition of 2% trifluroacetic acid. Peptides were separated by isoelectric focusing into 24 fractions on a 3100 OFFGEL Fractionator (Agilent, GmbH, Böblingen, Germany) as described in Ref. 45 (link). Each fraction was purified with C₁₈ StageTips (46 (link)) and analyzed via liquid chromatography combined with electrospray tandem mass spectrometry on an LTQ Orbitrap (Thermo Fisher) with lock mass calibration (47 (link)). All raw files were searched against the human and E. coli complete proteome sequences obtained from UniProt (version from January 2013) and a set of commonly observed contaminants. MS/MS spectra were filtered to contain at most eight peaks per 100 mass unit intervals. The initial MS mass tolerance was 20 ppm, and MS/MS fragment ions could deviate by up to 0.5 Da (48 (link)). For quantification, intensities can be determined alternatively as the full peak volume or as the intensity maximum over the retention time profile, and the latter method was used here as the default. Intensities of different isotopic peaks in an isotope pattern are always summed up for further analysis. MaxQuant offers a choice of the degree of uniqueness required in order for peptides to be included for quantification: “all peptides,” “only unique peptides,” and “unique plus razor peptides” (42 (link)). Here we chose the latter, because it is a good compromise between the two competing interests of using only peptides that undoubtedly belong to a protein and using as many peptide signals as possible. The distribution of peptide ions over fractions and samples is shown in supplemental Fig. S1.

Cox J., Hein M.Y., Luber C.A., Paron I., Nagaraj N, & Mann M. (2014). Accurate Proteome-wide Label-free Quantification by Delayed Normalization and Maximal Peptide Ratio Extraction, Termed MaxLFQ. Molecular & Cellular Proteomics : MCP, 13(9), 2513-2526.

Publication 2014

Acids Antibiotics, Antitubercular Biological Assay Buffers Cells Centrifugation Chloroform Cold Temperature Deoxycholic Acid, Monosodium Salt Digestion Dithiothreitol Edetic Acid Escherichia coli Escherichia coli K12 Glutamine HeLa Cells HEPES Homo sapiens Immune Tolerance Iodoacetamide Ions Isotopes Liquid Chromatography Methanol Peptides Promega Protease Inhibitors Proteins Proteome Radioimmunoprecipitation Assay Retention (Psychology) Sodium Chloride Staphylococcal Protein A Tandem Mass Spectrometry Thiourea Tromethamine Trypsin Urea

Efficient Electroporation and Cryopreservation of Mouse ES Cells

Cited 173 times

The final targeting constructs were prepared for ES cell electroporation from 2 ml of culture (2X LB plus antibiotics) in 96-well format using the Qiagen Turboprep kit. Before electroporation, vectors were linearized with AsiSI and examined by gel electrophoresis. For most clones, the digested DNA migrated as a single high-molecular-mass band of the expected size (Supplementary Fig. 5). Occasionally, contaminating smaller molecular mass bands were also observed on the gel (DNA quality failures).
JM8 mouse ES cell lines derived from the C57BL/6N strain were grown either on a feeder layer of SNL6/7 fibroblasts (neomycin and/or puromycin resistant) or on gelatinized tissue culture plates^{16 (link)}. Both feeder-independent and feeder-dependent lines were maintained in Knockout DMEM (500 ml, Gibco) supplemented with 2 mM glutamine, 5 ml 100× β-mercaptoethanol (360 μl in 500 ml PBS, filter sterilized), 10–15% fetal calf serum respectively (Invitrogen) and 500 U ml⁻¹ leukaemia-inhibitory factor (ESGRO, Millipore). Trypsin solution was prepared by adding 20 ml of 2.5% trypsin solution (Gibco) and 5 ml chicken serum (Gibco) to 500 ml filter-sterilized PBS containing 0.1 g EDTA (Sigma) and 0.5 g d-glucose (Sigma).
Electroporations of ES cells were carried out in a 25-well cuvette using the ECM 630 96-well electroporator /HT-200 automatic plate handler (BTX Harvard Apparatus; set at 700 V, 400 Ω, 25 μF). Immediately before electroporation, cell suspensions of ~1 × 10⁷ cells and ~2 μg of linearized targeting vector DNA were mixed in a final volume of 120 μl PBS. Cells were seeded onto a 10-cm dish (with feeders or gelatin) and colonies were picked after 10 d of selection in 100 μg (active) per ml Geneticin (Invitrogen). To expand cells into duplicate wells for archiving and preparation of genomic DNA, confluent cultures of JM8 ES cells grown on feeder cells were washed twice with pre-warmed PBS and trypsinized for 15 min at 37 °C. Five volumes of pre-warmed media were added and the cells were gently dispersed by tituration and passed at a dilution of 1:4 into new plates containing feeder cells. Passage of cells grown on gelatinized plates was carried out in a similar manner except that the cells were trypsinized for 10 min and passed at a dilution of 1:6 into freshly gelatin-coated plates (0.1% gelatin, Sigma G1393). Culture medium was replaced daily and cells reached confluence 2 days after passage. To archive ES cell clones, trypsinized cells from confluent 96-well plates were transferred in 200 μl freezing medium (Knockout DMEM, 15% serum/ 10% DMSO) to 96-well cryovials (Matrix) and overlayed with sterile mineral oil. The cells were placed at −80 °C overnight and then transferred to liquid nitrogen.

Skarnes W.C., Rosen B., West A.P., Koutsourakis M., Bushell W., Iyer V., Mujica A.O., Thomas M., Harrow J., Cox T., Jackson D., Severin J., Biggs P., Fu J., Nefedov M., de Jong P.J., Stewart A.F, & Bradley A. (2011). A conditional knockout resource for the genome–wide study of mouse gene function. Nature, 474(7351), 337-342.

Publication 2011

2-Mercaptoethanol Antibiotics Cells Chickens Clone Cells Cloning Vectors Edetic Acid Electrophoresis Electroporation Embryonic Stem Cells Feeder Cell Layers Feeder Cells Fetal Bovine Serum Fibroblasts Gelatins Geneticin Genome Glucose Glutamine Hyperostosis, Diffuse Idiopathic Skeletal LIF protein, human Mus Neomycin Nitrogen Oil, Mineral PRSS2 protein, human Puromycin Serum Sterility, Reproductive Strains Sulfoxide, Dimethyl Technique, Dilution Tissues Trypsin

Establishment and Characterization of UM-SCC Cell Lines

Cited 129 times

All of the UM-SCC cell lines were established from head and neck cancer patients who gave written informed consent in studies reviewed and approved by the University of Michigan Medical School Institutional Review Board. Current and early passage human UM-SCC cell lines established at the University of Michigan ^{(1 –3 (link), 5 (link), 30 (link))} were retrieved from liquid nitrogen storage. Cell lines were grown in complete Dulbecco’s Modified Eagle’s Medium (cDMEM) containing 2 mM L-glutamine, 1% nonessential amino acids, 1% Penicillin-Streptomycin (Invitrogen, Carlsbad, CA) and 10% fetal bovine serum, in a humidified atmosphere of 5% CO₂ at 37°C. All cell lines were tested for mycoplasma, using the MycoAlert Detection Kit (Cambrex, Rockland, ME). Contaminated cultures were treated with Plasmocin according to the manufacturer’s protocol, and testing was repeated at monthly intervals.

Brenner J.C., Graham M.P., Kumar B., Saunders L.M., Kupfer R., Lyons R.H., Bradford C.R, & Carey T.E. (2010). Genotyping of 73 UM-SCC head and neck squamous cell carcinoma cell lines. Head & neck, 32(4), 417-426.

Publication 2010

Amino Acids Atmosphere Cancer of Head and Neck Cell Lines Eagle Ethics Committees, Research Fetal Bovine Serum Glutamine Homo sapiens Mycoplasma Nitrogen Patients Penicillins plasmocin Streptomycin

Monocyte differentiation and activation

Cited 103 times

PBMC (1 × 10⁶/mL) are cultured in RPMI 1640 supplemented with 10% human serum, 2 mM L-glutamine, and 1% penicillin (Invitrogen Ltd, Paisley, UK) and incubated at 37°C in a humidified 5% CO₂ atmosphere for 2 h in a 12-well plate. After 2 h, non-adhering PBMCs are harvested and discarded; monocytes (adhering cells) are culture in medium alone (unstimulated) or primed with 2 μg/mL LPS for 2 h (Sigma–Aldrich, St. Louis, MO) before stimulation with Nigericine (5 μM) (Sigma–Aldrich) for 1 h at 37°C in a humidified 5% CO₂ atmosphere. Adhering cells (monocytes) are then collected by trypsin treatment and prepared for FlowSight analysis by immunofluorescence staining as THP1-derived macrophage (see above).

Cossarizza A., Chang H.D., Radbruch A., Acs A., Adam D., Adam-Klages S., Agace W.W., Aghaeepour N., Akdis M., Allez M., Almeida L.N., Alvisi G., Anderson G., Andrä I., Annunziato F., Anselmo A., Bacher P., Baldari C.T., Bari S., Barnaba V., Barros-Martins J., Battistini L., Bauer W., Baumgart S., Baumgarth N., Baumjohann D., Baying B., Bebawy M., Becher B., Beisker W., Benes V., Beyaert R., Blanco A., Boardman D.A., Bogdan C., Borger J.G., Borsellino G., Boulais P.E., Bradford J.A., Brenner D., Brinkman R.R., Brooks A.E., Busch D.H., Büscher M., Bushnell T.P., Calzetti F., Cameron G., Cammarata I., Cao X., Cardell S.L., Casola S., Cassatella M.A., Cavani A., Celada A., Chatenoud L., Chattopadhyay P.K., Chow S., Christakou E., Čičin-Šain L., Clerici M., Colombo F.S., Cook L., Cooke A., Cooper A.M., Corbett A.J., Cosma A., Cosmi L., Coulie P.G., Cumano A., Cvetkovic L., Dang V.D., Dang-Heine C., Davey M.S., Davies D., De Biasi S., Del Zotto G., Cruz G.V., Delacher M., Bella S.D., Dellabona P., Deniz G., Dessing M., Di Santo J.P., Diefenbach A., Dieli F., Dolf A., Dörner T., Dress R.J., Dudziak D., Dustin M., Dutertre C.A., Ebner F., Eckle S.B., Edinger M., Eede P., Ehrhardt G.R., Eich M., Engel P., Engelhardt B., Erdei A., Esser C., Everts B., Evrard M., Falk C.S., Fehniger T.A., Felipo-Benavent M., Ferry H., Feuerer M., Filby A., Filkor K., Fillatreau S., Follo M., Förster I., Foster J., Foulds G.A., Frehse B., Frenette P.S., Frischbutter S., Fritzsche W., Galbraith D.W., Gangaev A., Garbi N., Gaudilliere B., Gazzinelli R.T., Geginat J., Gerner W., Gherardin N.A., Ghoreschi K., Gibellini L., Ginhoux F., Goda K., Godfrey D.I., Goettlinger C., González-Navajas J.M., Goodyear C.S., Gori A., Grogan J.L., Grummitt D., Grützkau A., Haftmann C., Hahn J., Hammad H., Hämmerling G., Hansmann L., Hansson G., Harpur C.M., Hartmann S., Hauser A., Hauser A.E., Haviland D.L., Hedley D., Hernández D.C., Herrera G., Herrmann M., Hess C., Höfer T., Hoffmann P., Hogquist K., Holland T., Höllt T., Holmdahl R., Hombrink P., Houston J.P., Hoyer B.F., Huang B., Huang F.P., Huber J.E., Huehn J., Hundemer M., Hunter C.A., Hwang W.Y., Iannone A., Ingelfinger F., Ivison S.M., Jäck H.M., Jani P.K., Jávega B., Jonjic S., Kaiser T., Kalina T., Kamradt T., Kaufmann S.H., Keller B., Ketelaars S.L., Khalilnezhad A., Khan S., Kisielow J., Klenerman P., Knopf J., Koay H.F., Kobow K., Kolls J.K., Kong W.T., Kopf M., Korn T., Kriegsmann K., Kristyanto H., Kroneis T., Krueger A., Kühne J., Kukat C., Kunkel D., Kunze-Schumacher H., Kurosaki T., Kurts C., Kvistborg P., Kwok I., Landry J., Lantz O., Lanuti P., LaRosa F., Lehuen A., LeibundGut-Landmann S., Leipold M.D., Leung L.Y., Levings M.K., Lino A.C., Liotta F., Litwin V., Liu Y., Ljunggren H.G., Lohoff M., Lombardi G., Lopez L., López-Botet M., Lovett-Racke A.E., Lubberts E., Luche H., Ludewig B., Lugli E., Lunemann S., Maecker H.T., Maggi L., Maguire O., Mair F., Mair K.H., Mantovani A., Manz R.A., Marshall A.J., Martínez-Romero A., Martrus G., Marventano I., Maslinski W., Matarese G., Mattioli A.V., Maueröder C., Mazzoni A., McCluskey J., McGrath M., McGuire H.M., McInnes I.B., Mei H.E., Melchers F., Melzer S., Mielenz D., Miller S.D., Mills K.H., Minderman H., Mjösberg J., Moore J., Moran B., Moretta L., Mosmann T.R., Müller S., Multhoff G., Muñoz L.E., Münz C., Nakayama T., Nasi M., Neumann K., Ng L.G., Niedobitek A., Nourshargh S., Núñez G., O’Connor J.E., Ochel A., Oja A., Ordonez D., Orfao A., Orlowski-Oliver E., Ouyang W., Oxenius A., Palankar R., Panse I., Pattanapanyasat K., Paulsen M., Pavlinic D., Penter L., Peterson P., Peth C., Petriz J., Piancone F., Pickl W.F., Piconese S., Pinti M., Pockley A.G., Podolska M.J., Poon Z., Pracht K., Prinz I., Pucillo C.E., Quataert S.A., Quatrini L., Quinn K.M., Radbruch H., Radstake T.R., Rahmig S., Rahn H.P., Rajwa B., Ravichandran G., Raz Y., Rebhahn J.A., Recktenwald D., Reimer D., e Sousa C.R., Remmerswaal E.B., Richter L., Rico L.G., Riddell A., Rieger A.M., Robinson J.P., Romagnani C., Rubartelli A., Ruland J., Saalmüller A., Saeys Y., Saito T., Sakaguchi S., de-Oyanguren F.S., Samstag Y., Sanderson S., Sandrock I., Santoni A., Sanz R.B., Saresella M., Sautes-Fridman C., Sawitzki B., Schadt L., Scheffold A., Scherer H.U., Schiemann M., Schildberg F.A., Schimisky E., Schlitzer A., Schlosser J., Schmid S., Schmitt S., Schober K., Schraivogel D., Schuh W., Schüler T., Schulte R., Schulz A.R., Schulz S.R., Scottá C., Scott-Algara D., Sester D.P., Shankey T.V., Silva-Santos B., Simon A.K., Sitnik K.M., Sozzani S., Speiser D.E., Spidlen J., Stahlberg A., Stall A.M., Stanley N., Stark R., Stehle C., Steinmetz T., Stockinger H., Takahama Y., Takeda K., Tan L., Tárnok A., Tiegs G., Toldi G., Tornack J., Traggiai E., Trebak M., Tree T.I., Trotter J., Trowsdale J., Tsoumakidou M., Ulrich H., Urbanczyk S., van de Veen W., van den Broek M., van der Pol E., Van Gassen S., Van Isterdael G., van Lier R.A., Veldhoen M., Vento-Asturias S., Vieira P., Voehringer D., Volk H.D., von Borstel A., von Volkmann K., Waisman A., Walker R.V., Wallace P.K., Wang S.A., Wang X.M., Ward M.D., Ward-Hartstonge K.A., Warnatz K., Warnes G., Warth S., Waskow C., Watson J.V., Watzl C., Wegener L., Weisenburger T., Wiedemann A., Wienands J., Wilharm A., Wilkinson R.J., Willimsky G., Wing J.B., Winkelmann R., Winkler T.H., Wirz O.F., Wong A., Wurst P., Yang J.H., Yang J., Yazdanbakhsh M., Yu L., Yue A., Zhang H., Zhao Y., Ziegler S.M., Zielinski C., Zimmermann J, & Zychlinsky A. (2019). Guidelines for the use of flow cytometry and cell sorting in immunological studies (second edition). European journal of immunology, 49(10), 1457-1973.

Publication 2019

Atmosphere Cells Culture Media Glutamine Homo sapiens Immunofluorescence Macrophage Monocytes Penicillins Serum Trypsin

Bone Marrow-Derived Macrophage Generation

Cited 95 times

Fresh or frozen bone marrow cells were used to generate BMDM as previously described [8] (link), using L929-cell conditioned medium (LCCM) as a source of granulocyte/macrophage colony stimulating factor [9] (link). The cells were resuspended in 10 ml bone marrow differentiation media (R20/30), which is RPMI1640 supplemented with 20% fetal bovine serum (Gibco, cat. 12657-029), 30% LCCM, 100 U/ml penicillin, 100 µg/ml streptomycin, and 2 mM L-glutamine. Cells were seeded in non-tissue culture treated Optilux Petri dishes (BD Biosciences) and incubated at 37°C in a 5% CO₂ atmosphere. Four days after seeding the cells, an extra 10 ml of fresh R20/30 were added per plate and incubated for an additional 3 days. To obtain the BMDM, the supernatants were discarded and the attached cells were washed with 10 ml of sterile PBS. Ten ml of ice-cold PBS were added to each plate and incubated at 4°C for 10 minutes. The macrophages were detached by gently pipetting the PBS across the dish. The cells were centrifuged at 200× g for 5 minutes and resuspended in 10 ml of BMDM cultivation media (R10/5), which is composed of RPMI 1640, 10% fetal bovine serum, 5% LCCM and 2 mM L-glutamine. The cells were counted, seeded and cultivated in tissue culture plates 12 hours before any further experimental procedure.

Marim F.M., Silveira T.N., Lima DS J.r, & Zamboni D.S. (2010). A Method for Generation of Bone Marrow-Derived Macrophages from Cryopreserved Mouse Bone Marrow Cells. PLoS ONE, 5(12), e15263.

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Publication 2010

Atmosphere Bone Marrow Bone Marrow Cells Cells Common Cold Culture Media, Conditioned Fetal Bovine Serum Freezing Glutamine Granulocyte-Macrophage Colony-Stimulating Factor Hyperostosis, Diffuse Idiopathic Skeletal L929 Cells Macrophage Penicillins Sterility, Reproductive Streptomycin Tissues

Most recents protocols related to «Glutamine»

Quantifying IL-2 Effects on T Cell Activation

Not available on PMC !

Example 7

Impact of IL-2 signalling on Teff responses is characterised in a T cell activation assay, in which intracellular granzyme B (GrB) upregulation and proliferation are examined. Previously frozen primary human Pan T cells (Stemcell Technologies) are labelled with eFluor450 cell proliferation dye (Invitrogen) according to manufacturer's recommendation, and added to 96-U-bottom well plates at 1×10⁵cells/well in RPMI 1640 (Life Technologies) containing 10% FBS (Sigma), 2 mM L-Glutamine (Life Technologies) and 10,000 U/ml Pen-Strep (Sigma). The cells are then treated with 10 μg/ml anti-CD25 antibodies or control antibodies followed by Human T-Activator CD3/CD28 (20:1 cell to bead ratio; Gibco) and incubated for 72 hrs in a 37° C., 5% CO₂humidified incubator. To assess T cell activation, cells are stained with the eBioscience Fixable Viability Dye efluor780 (Invitrogen), followed by fluorochrome labelled antibodies for surface T cell markers (CD3-PerCP-Cy5.5 clone UCHT1 Biolegend, CD4-BV510 clone SK3 BD Bioscience, CD8-Alexa Fluor 700 clone RPA-T8 Invitrogen, CD45RA-PE-Cy7 clone HI100 Invitrogen, CD25-BUV737 clone 2A3 BD Bioscience) and then fixed and permeabilized with the eBioscience™ Foxp3/Transcription Factor Staining Buffer Set (Invitrogen) before staining for intracellular GrB and intranuclear FoxP3 (Granzyme B-PE clone GB11 BD Bioscience, FoxP3-APC clone 236A/E7). Samples are acquired on the Fortessa LSR X20 Flow Cytometer (BD Bioscience) and analysed using the BD FACSDIVA software. Doublets are excluded using FCS-H versus FCS-A, and lymphocytes defined using SSC-A versus FCS-A parameters. CD4⁺ and CD8⁺ T cell subsets gated from the live CD3+ lymphocytes are assessed using a GrB-PE-A versus proliferation eFluor450-A plot. Results are presented as percentage of proliferating GrB positive cells from the whole CD4⁺ T cell population. Graphs and statistical analysis is performed using GraphPad Prism v7. (results not shown)

US11873341B2. Anti-CD25 for tumour specific cell depletion (2024-01-16). Tusk Therapeutics Ltd. [GB], Cancer Research Technology Limited [GB]. Inventors: Anne Goubier [GB], Beatriz Goyenechea Corzo [GB], Josephine Salimu [GB], Kevin Moulder [GB], Pascal Merchiers [GB], Sergio Quezada [GB].

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Patent 2024

Anti-Antibodies Antibodies Biological Assay Buffers CD4 Positive T Lymphocytes Cell Proliferation Cells Clone Cells CY5.5 cyanine dye Eragrostis Fluorescent Dyes Freezing Glutamine GZMB protein, human Homo sapiens IL2RA protein, human Lymphocyte prisma Protoplasm Stem Cells Streptococcal Infections T-Lymphocyte T-Lymphocyte Subsets Transcriptional Activation Transcription Factor

Microbial Seed Treatments for Enhanced Crop Performance

Not available on PMC !

Example 2

A. Seed Treatment with Isolated Microbe

In this example, an isolated microbe from Tables 1-3 will be applied as a seed coating to seeds of corn (Zea mays). Upon applying the isolated microbe as a seed coating, the corn will be planted and cultivated in the standard manner.

A control plot of corn seeds, which did not have the isolated microbe applied as a seed coating, will also be planted.

It is expected that the corn plants grown from the seeds treated with the seed coating will exhibit a quantifiably higher biomass than the control corn plants.

The biomass from the treated plants may be about 1-10% higher, 10-20% higher, 20-30% higher, 30-40% higher, 40-50% higher, 50-60% higher, 60-70% higher, 70-80% higher, 80-90% higher, or more.

The biomass from the treated plants may equate to about a 1 bushel per acre increase over the controls, or a 2 bushel per acre increase, or a 3 bushel per acre increase, or a 4 bushel per acre increase, or a 5 bushel per acre increase, or more.

In some aspects, the biomass increase is statistically significant. In other aspects, the biomass increase is not statistically significant, but is still quantifiable.

B. Seed Treatment with Microbial Consortia

In this example, a microbial consortium, comprising at least two microbes from Tables 1-3 will be applied as a seed coating to seeds of corn (Zea mays). Upon applying the microbial consortium as a seed coating, the corn will be planted and cultivated in the standard manner.

A control plot of corn seeds, which did not have the microbial consortium applied as a seed coating, will also be planted.

It is expected that the corn plants grown from the seeds treated with the seed coating will exhibit a quantifiably higher biomass than the control corn plants.

The biomass from the treated plants may be about 1-10% higher, 10-20% higher, 20-30% higher, 30-40% higher, 40-50% higher, 50-60% higher, 60-70% higher, 70-80% higher, 80-90% higher, or more.

In some aspects, the biomass increase is statistically significant. In other aspects, the biomass increase is not statistically significant, but is still quantifiable.

C. Treatment with Agricultural Composition Comprising Isolated Microbe

In this example, an isolated microbe from Tables 1-3 will be applied as an agricultural composition, administered to the corn seed at the time of sowing.

For example, it is anticipated that a farmer will apply the agricultural composition to the corn seeds simultaneously upon planting the seeds into the field. This can be accomplished, for example, by applying the agricultural composition to a hopper/bulk tank on a standard 16 row planter, which contains the corn seeds and which is configured to plant the same into rows. Alternatively, the agricultural composition can be contained in a separate bulk tank on the planter and sprayed into the rows upon planting the corn seed.

A control plot of corn seeds, which are not administered the agricultural composition, will also be planted.

It is expected that the corn plants grown from the seeds treated with the agricultural composition will exhibit a quantifiably higher biomass than the control corn plants.

The biomass from the treated plants may be about 1-10% higher, 10-20% higher, 20-30% higher, 30-40% higher, 40-50% higher, 50-60% higher, 60-70% higher, 70-80% higher, 80-90% higher, or more.

In some aspects, the biomass increase is statistically significant. In other aspects, the biomass increase is not statistically significant, but is still quantifiable.

D. Treatment with Agricultural Composition Comprising Microbial Consortia

In this example, a microbial consortium, comprising at least two microbes from Tables 1-3 will be applied as an agricultural composition, administered to the corn seed at the time of sowing.

A control plot of corn seeds, which are not administered the agricultural composition, will also be planted.

It is expected that the corn plants grown from the seeds treated with the agricultural composition will exhibit a quantifiably higher biomass than the control corn plants.

The biomass from the treated plants may be about 1-10% higher, 10-20% higher, 20-30% higher, 30-40% higher, 40-50% higher, 50-60% higher, 60-70% higher, 70-80% higher, 80-90% higher, or more.

In some aspects, the biomass increase is statistically significant. In other aspects, the biomass increase is not statistically significant, but is still quantifiable.

A. Seed Treatment with Isolated Microbe

A control plot of corn seeds, which did not have the isolated microbe applied as a seed coating, will also be planted.

It is expected that the corn plants grown from the seeds treated with the seed coating will exhibit a quantifiable and superior ability to tolerate drought conditions and/or exhibit superior water use efficiency, as compared to the control corn plants.

The drought tolerance and/or water use efficiency can be based on any number of standard tests from the art, e.g leaf water retention, turgor loss point, rate of photosynthesis, leaf color and other phenotypic indications of drought stress, yield performance, and various root morphological and growth patterns.

B. Seed Treatment with Microbial Consortia

A control plot of corn seeds, which did not have the microbial consortium applied as a seed coating, will also be planted.

C. Treatment with Agricultural Composition Comprising Isolated Microbe

In this example, an isolated microbe from Tables 1-3 will be applied as an agricultural composition, administered to the corn seed at the time of sowing.

A control plot of corn seeds, which are not administered the agricultural composition, will also be planted.

It is expected that the corn plants grown from the seeds treated with the with the agricultural composition will exhibit a quantifiable and superior ability to tolerate drought conditions and/or exhibit superior water use efficiency, as compared to the control corn plants.

D. Treatment with Agricultural Composition Comprising Microbial Consortia

In this example, a microbial consortium, comprising at least two microbes from Tables 1-3 will be applied as an agricultural composition, administered to the corn seed at the time of sowing.

A control plot of corn seeds, which are not administered the agricultural composition, will also be planted.

A. Seed Treatment with Isolated Microbe

A control plot of corn seeds, which did not have the isolated microbe applied as a seed coating, will also be planted.

It is expected that the corn plants grown from the seeds treated with the seed coating will exhibit a quantifiable and superior ability to utilize nitrogen, as compared to the control corn plants.

The nitrogen use efficiency can be quantified by recording a measurable change in any of the main nitrogen metabolic pool sizes in the assimilation pathways (e.g., a measurable change in one or more of the following: nitrate, nitrite, ammonia, glutamic acid, aspartic acid, glutamine, asparagine, lysine, leucine, threonine, methionine, glycine, tryptophan, tyrosine, total protein content of a plant part, total nitrogen content of a plant part, and/or chlorophyll content), or where the treated plant is shown to provide the same or elevated biomass or harvestable yield at lower nitrogen fertilization levels compared to the control plant, or where the treated plant is shown to provide elevated biomass or harvestable yields at the same nitrogen fertilization levels compared to a control plant.

B. Seed Treatment with Microbial Consortia

A control plot of corn seeds, which did not have the microbial consortium applied as a seed coating, will also be planted.

It is expected that the corn plants grown from the seeds treated with the seed coating will exhibit a quantifiable and superior ability to utilize nitrogen, as compared to the control corn plants.

C. Treatment with Agricultural Composition Comprising Isolated Microbe

In this example, an isolated microbe from Tables 1-3 will be applied as an agricultural composition, administered to the corn seed at the time of sowing.

A control plot of corn seeds, which are not administered the agricultural composition, will also be planted.

It is expected that the corn plants grown from the seeds treated with the agricultural composition will exhibit a quantifiable and superior ability to utilize nitrogen, as compared to the control corn plants.

D. Treatment with Agricultural Composition Comprising Microbial Consortia

In this example, a microbial consortium, comprising at least two microbes from Tables 1-3 will be applied as an agricultural composition, administered to the corn seed at the time of sowing.

A control plot of corn seeds, which are not administered the agricultural composition, will also be planted.

The inoculants were prepared from isolates grown as spread plates on R2A incubated at 25° C. for 48 to 72 hours. Colonies were harvested by blending with sterile distilled water (SDW) which was then transferred into sterile containers. Serial dilutions of the harvested cells were plated and incubated at 25° C. for 24 hours to estimate the number of colony forming units (CFU) in each suspension. Dilutions were prepared using individual isolates or blends of isolates (consortia) to deliver 1×10⁵cfu/microbe/seed and seeds inoculated by either imbibition in the liquid suspension or by overtreatment with 5% vegetable gum and oil.

Seeds corresponding to the plants of table 15 were planted within 24 to 48 hours of treatment in agricultural soil, potting media or inert growing media. Plants were grown in small pots (28 mL to 200 mL) in either a controlled environment or in a greenhouse. Chamber photoperiod was set to 16 hours for all experiments on all species. Air temperature was typically maintained between 22-24° C.

Unless otherwise stated, all plants were watered with tap water 2 to 3 times weekly. Growth conditions were varied according to the trait of interest and included manipulation of applied fertilizer, watering regime and salt stress as follows:

- Low N—seeds planted in soil potting media or inert growing media with no applied N fertilizer
- Moderate N—seeds planted in soil or growing media supplemented with commercial N fertilizer to equivalent of 135 kg/ha applied N
- Insol P—seeds planted in potting media or inert growth substrate and watered with quarter strength Pikovskaya's liquid medium containing tri-calcium phosphate as the only form phosphate fertilizer.
- Cold Stress—seeds planted in soil, potting media or inert growing media and incubated at 10° C. for one week before being transferred to the plant growth room.
- Salt stress—seeds planted in soil, potting media or inert growing media and watered with a solution containing between 100 to 200 mg/L NaCl.

Untreated (no applied microbe) controls were prepared for each experiment. Plants were randomized on trays throughout the growth environment. Between 10 and 30 replicate plants were prepared for each treatment in each experiment. Phenotypes were measured during early vegetative growth, typically before the V3 developmental stage and between 3 and 6 weeks after sowing. Foliage was cut and weighed. Roots were washed, blotted dry and weighed. Results indicate performance of treatments against the untreated control.

TABLE 15

StrainShootRoot

Microbe sp.IDCropAssayIOC (%)IOC (%)

Bosea thiooxidans123EfficacyEfficacy

overall100%100%

Bosea thiooxidans54522WheatEarly vigor - insol P30-40 —

Bosea thiooxidans54522RyegrassEarly vigor50-60 50-60

Bosea thiooxidans54522RyegrassEarly vigor - moderate P0-100-10

Duganella violaceinigra111EfficacyEfficacy

overall100%100%

Duganella violaceinigra66361TomatoEarly vigor0-100-10

Duganella violaceinigra66361TomatoEarly vigor30-40 40-50

Duganella violaceinigra66361TomatoEarly vigor20-30 20-30

Herbaspirillum huttiense222Efficacy—

overall100%

Herbaspirillum huttiense54487WheatEarly vigor - insol P30-40 —

Herbaspirillum huttiense60507MaizeEarly vigor - salt stress0-100-10

Janthinobacterium sp.222Efficacy—

Overall100%

Janthinobacterium sp.54456WheatEarly vigor - insol P30-40 —

Janthinobacterium sp.54456WheatEarly vigor - insol P0-10—

Janthinobacterium sp.63491RyegrassEarly vigor - drought0-100-10

stress

Massilia niastensis112EfficacyEfficacy

overall80%80%

Massilia niastensis55184WheatEarly vigor - salt stress0-1020-30

Massilia niastensis55184WinterEarly vigor - cold stress0-1010-20

wheat

Massilia niastensis55184WinterEarly vigor - cold stress20-30 20-30

wheat

Massilia niastensis55184WinterEarly vigor - cold stress10-20 10-20

wheat

Massilia niastensis55184WinterEarly vigor - cold stress<0<0

wheat

Novosphingobium rosa211EfficacyEfficacy

overall100%100%

Novosphingobium rosa65589MaizeEarly vigor - cold stress0-100-10

Novosphingobium rosa65619MaizeEarly vigor - cold stress0-100-10

Paenibacillus amylolyticus111EfficacyEfficacy

overall100%100%

Paenibacillus amylolyticus66316TomatoEarly vigor0-100-10

Paenibacillus amylolyticus66316TomatoEarly vigor10-20 10-20

Paenibacillus amylolyticus66316TomatoEarly vigor0-100-10

Pantoea agglomerans323EfficacyEfficacy

33%50%

Pantoea agglomerans54499WheatEarly vigor - insol P40-50 —

Pantoea agglomerans57547MaizeEarly vigor - low N<00-10

Pantoea vagans55529MaizeEarly vigor<0<0

(formerly P. agglomerans)

Polaromonas ginsengisoli111EfficacyEfficacy

66%100%

Polaromonas ginsengisoli66373TomatoEarly vigor0-100-10

Polaromonas ginsengisoli66373TomatoEarly vigor20-30 30-40

Polaromonas ginsengisoli66373TomatoEarly vigor<010-20

Pseudomonas fluorescens122Efficacy—

100%

Pseudomonas fluorescens54480WheatEarly vigor - insol P>100 —

Pseudomonas fluorescens56530MaizeEarly vigor - moderate N0-10—

Rahnella aquatilis334EfficacyEfficacy

80%63%

Rahnella aquatilis56532MaizeEarly vigor - moderate N10-20 —

Rahnella aquatilis56532MaizeEarly vigor - moderate N0-100-10

Rahnella aquatilis56532WheatEarly vigor - cold stress0-1010-20

Rahnella aquatilis56532WheatEarly vigor - cold stress<00-10

Rahnella aquatilis56532WheatEarly vigor - cold stress10-20 <0

Rahnella aquatilis57157RyegrassEarly vigor<0—

Rahnella aquatilis57157MaizeEarly vigor - low N0-100-10

Rahnella aquatilis57157MaizeEarly vigor - low N0-10<0

Rahnella aquatilis58013MaizeEarly vigor0-1010-20

Rahnella aquatilis58013MaizeEarly vigor - low N0-10<0

Rhodococcus erythropolis313Efficacy—

66%

Rhodococcus erythropolis54093MaizeEarly vigor - low N40-50 —

Rhodococcus erythropolis54299MaizeEarly vigor - insol P>100 —

Rhodococcus erythropolis54299MaizeEarly vigor<0<0

Stenotrophomonas chelatiphaga611EfficacyEfficacy

60%60%

Stenotrophomonas chelatiphaga54952MaizeEarly vigor0-100-10

Stenotrophomonas chelatiphaga47207MaizeEarly vigor<0 0

Stenotrophomonas chelatiphaga64212MaizeEarly vigor0-1010-20

Stenotrophomonas chelatiphaga64208MaizeEarly vigor0-100-10

Stenotrophomonas chelatiphaga58264MaizeEarly vigor<0<0

Stenotrophomonas maltophilia612EfficacyEfficacy

43%66%

Stenotrophomonas maltophilia54073MaizeEarly vigor - low N50-60 —

Stenotrophomonas maltophilia54073MaizeEarly vigor<00-10

Stenotrophomonas maltophilia56181MaizeEarly vigor0-10<0

Stenotrophomonas maltophilia54999MaizeEarly vigor0-100-10

Stenotrophomonas maltophilia54850MaizeEarly vigor 00-10

Stenotrophomonas maltophilia54841MaizeEarly vigor<00-10

Stenotrophomonas maltophilia46856MaizeEarly vigor<0<0

Stenotrophomonas rhizophila811EfficacyEfficacy

12.5%37.5%

Stenotrophomonas rhizophila50839MaizeEarly vigor<0<0

Stenotrophomonas rhizophila48183MaizeEarly vigor<0<0

Stenotrophomonas rhizophila45125MaizeEarly vigor<0<0

Stenotrophomonas rhizophila46120MaizeEarly vigor<00-10

Stenotrophomonas rhizophila46012MaizeEarly vigor<0<0

Stenotrophomonas rhizophila51718MaizeEarly vigor0-100-10

Stenotrophomonas rhizophila66478MaizeEarly vigor<0<0

Stenotrophomonas rhizophila65303MaizeEarly vigor<00-10

Stenotrophomonas terrae221EfficacyEfficacy

50%50%

Stenotrophomonas terrae68741MaizeEarly vigor<0<0

Stenotrophomonas terrae68599MaizeEarly vigor<00-10

Stenotrophomonas terrae68599Capsicum *Early vigor20-30 20-30

Stenotrophomonas terrae68741Capsicum *Early vigor10-20 20-30

The data presented in table 15 describes the efficacy with which a microbial species or strain can change a phenotype of interest relative to a control run in the same experiment. Phenotypes measured were shoot fresh weight and root fresh weight for plants growing either in the absence of presence of a stress (assay). For each microbe species, an overall efficacy score indicates the percentage of times a strain of that species increased a both shoot and root fresh weight in independent evaluations. For each species, the specifics of each independent assay is given, providing a strain ID (strain) and the crop species the assay was performed on (crop). For each independent assay the percentage increase in shoot and root fresh weight over the controls is given.

US11871752B2. Agriculturally beneficial microbes, microbial compositions, and consortia (2024-01-16). BIOCONSORTIA, INC. [US]. Inventors: Peter Wigley [NZ], Susan Turner [US], Caroline George [NZ], Thomas Williams [US], Kelly Roberts [US], Graham Hymus [US], Kelvin Lau [NZ].

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Patent 2024

Ammonia Asparagine Aspartic Acid Biological Assay Bosea thiooxidans Calcium Phosphates Capsicum Cells Chlorophyll Cold Shock Stress Cold Temperature Crop, Avian Dietary Fiber DNA Replication Droughts Drought Tolerance Embryophyta Environment, Controlled Farmers Fertilization Glutamic Acid Glutamine Glycine Growth Disorders Herbaspirillum Herbaspirillum huttiense Leucine Lolium Lycopersicon esculentum Lysine Maize Massilia niastensis Methionine Microbial Consortia Nitrates Nitrites Nitrogen Novosphingobium rosa Paenibacillus Paenibacillus amylolyticus Pantoea agglomerans Pantoea vagans Phenotype Phosphates Photosynthesis Plant Development Plant Embryos Plant Leaves Plant Proteins Plant Roots Plants Polaromonas ginsengisoli Pseudoduganella violaceinigra Pseudomonas Pseudomonas fluorescens Rahnella Rahnella aquatilis Retention (Psychology) Rhodococcus erythropolis Rosa Salt Stress Sodium Chloride Sodium Chloride, Dietary Stenotrophomonas chelatiphaga Stenotrophomonas maltophilia Stenotrophomonas rhizophila Stenotrophomonas terrae Sterility, Reproductive Strains Technique, Dilution Threonine Triticum aestivum Tryptophan Tyrosine Vegetables Zea mays

Directed Engineering of TpH2 Enzyme

Not available on PMC !

Example 2

Directed TpH Engineering

It was found that Homo sapiens TpH2, i.e., the fragment set forth as SEQ ID NO:13; hsTpH2, was sensitive to p-chlorophenylalanine. However, mutations at residues N97 and/or P99 were found to confer resistance to p-chlorophenylalanine and to exhibit improved 5HTP biosynthesis after growing cells in the presence of 100 mg/l of tryptophan overnight at 3TC. A further, saturated mutagenesis, study found that isoleucine (I) was a beneficial amino acid change at residue N97, while cysteine (C), aspartic acid (D), leucine (L) and glutamine (Q) were shown to be beneficial at residue P99. In particular, the combined changes 1\197I/P99D in hsTpH2 showed a >15% increase in 5HTP production in the presence of 100 mg/l tryptophan and the combined changes N97I/P99C in hsTpH2 showed a >25% increase in 5HTP biosynthesis, over the parent TPH2 sequence (SEQ ID NO:13) after acquiring the E2K mutation.

US11866749B2. Optimized microbial cells for production of melatonin and other compounds (2024-01-09). Danmarks Tekniske Universitet [DK]. Inventors: Hao Luo [DK], Jochen Förster [DK].

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Patent 2024

5-Hydroxytryptophan Amino Acids Anabolism Aspartic Acid Cells Cysteine Fenclonine Glutamine Homo sapiens Isoleucine Leucine Melatonin Mutagenesis Mutation Parent Tryptophan

Characterization of Plasmodium falciparum Glutamine Synthetase

Not available on PMC !

Example 2

Prokaryotic GS-I proteins found in some eukaryotes frequently display no GS catalytic activity and may have different functions. In humans, for example, most tissues/organs express only catalytically-active GS-II. In contrast, human GS-I does not exhibit GS activity. It is expressed only in the lens of the eye and has designated lengsin (lens GS-like protein), probably with a structural role.

To examine the catalytic activity of PfGS-I, PfGS-I gene was cloned and expressed in E. coli and then GS activity of the purified protein was assayed. PfGS-I produced glutamine from glutamate in the presence of ATP, Mg²⁺ and ammonia (FIG. 2A) demonstrates that PfGS-I is a functional GS.

US11877996B1. Arsinothricin as a multi-stage antimalarial (2024-01-23). None [US], None [US], None [US], None [US]. Inventors: Masafumi Yoshinaga [US], Barry P. Rosen [US], Jun Li [US], Guodong Niu [US].

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Patent 2024

Ammonia enzyme activity Escherichia coli Eukaryota Genes Glutamate Glutamine Homo sapiens Lens, Crystalline Prokaryotic Cells Proteins Synapsin I Tissues

Lentiviral Transduction of Jurkat Cells

Not available on PMC !

Example 2

CAR-T constructs in pLenti6.3/V5-DEST were purified using the PureLink HQ plasmid purification kit (Life Technology). CAR-T plasmids were lipofected into 293-FT cells with ViraPower packaging plasmids (Life Technologies) according to the manufacturer's protocol. After 48-72 hours, cell supernatant containing live Lentivirus was harvested. Optionally, the virus was concentrated using Lenti-X Concentrator (Clontech), according to the manufacturer's protocol.

Jurkat E6.1 cells were grown in RPMI (Sigma), 10% foetal bovine serum, 2 mM L-glutamine

Jurkat E6.1 cells were transduced for 48-72 hours with viral supernatant in a 50:50 mix of HEK cell supernatant:Jurkat medium: cells at a final concentration of 5×10⁵/ml.

A non-CAR-T construct containing the open reading frame of the Green Fluorescent Protein (GFP) was included as a control. Note that this construct gives cytoplasmic expression.

US11866510B2. Chimeric antigen receptor with single domain antibody (2024-01-09). CRESCENDO BIOLOGICS LIMITED [GB]. Inventors: Brian McGuinness [GB], Colette Johnston [GB].

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Patent 2024

Cells Cytoplasm Fetal Bovine Serum Glutamine Green Fluorescent Proteins Jurkat Cells Lentivirus Plasmids Virus

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L-glutamine is an amino acid that is commonly used as a dietary supplement and in cell culture media. It serves as a source of nitrogen and supports cellular growth and metabolism.

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Penicillin is a type of antibiotic used in laboratory settings. It is a broad-spectrum antimicrobial agent effective against a variety of bacteria. Penicillin functions by disrupting the bacterial cell wall, leading to cell death.

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Streptomycin is a broad-spectrum antibiotic used in laboratory settings. It functions as a protein synthesis inhibitor, targeting the 30S subunit of bacterial ribosomes, which plays a crucial role in the translation of genetic information into proteins. Streptomycin is commonly used in microbiological research and applications that require selective inhibition of bacterial growth.

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DMEM (Dulbecco's Modified Eagle's Medium) is a cell culture medium formulated to support the growth and maintenance of a variety of cell types, including mammalian cells. It provides essential nutrients, amino acids, vitamins, and other components necessary for cell proliferation and survival in an in vitro environment.

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L-glutamine is a laboratory-grade amino acid that serves as a key component in cell culture media. It provides a source of nitrogen and energy for cellular metabolism, supporting the growth and proliferation of cells in vitro.

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FBS, or Fetal Bovine Serum, is a commonly used cell culture supplement. It is derived from the blood of bovine fetuses and provides essential growth factors, hormones, and other nutrients to support the growth and proliferation of a wide range of cell types in vitro.

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Glutamine is a naturally occurring amino acid that plays a crucial role in various metabolic processes. It serves as a primary fuel source for rapidly dividing cells, such as those found in the intestines and immune system. Glutamine is also involved in the synthesis of other amino acids, proteins, and nucleic acids. As a laboratory reagent, it is commonly used in cell culture media to support the growth and proliferation of cells.

What are the main functions of glutamine in the body?

Glutamine is a highly versatile and important amino acid that plays crucial roles in various metabolic processes. It serves as a precursor for the synthesis of other amino acids, proteins, and nucleic acids. Glutamine is also involved in energy production, acid-base balance, and supporting the immune system. It is particularly important for the health and function of the gastrointestinal tract, muscle tissue, and the brain, making it essential for overall wellbeing and the body's natural healing and repair processes.

What are some of the potential therapeutic applications of glutamine supplementation?

Researchers continue to explore the potential therapeutic benefits of glutamine supplementation across a wide range of clinical conditions. Some areas of interest include sports performance, critical illness, and neurological disorders. Glutamine supplementation may help support muscle recovery, immune function, and cognitive function in certain populations. However, more research is needed to fully understand the specific applications and optimal dosing for various health conditions.

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PubCompare.ai is an innovative AI-driven platform that can help maximize the efficiency and effectiveness of your glutamine research. The platform allows you to screen protocol literature more efficiently, leveraging AI to pinpoint critical insights that can help you identify the most effective protocols related to glutamine for your specific research goals. The platform's AI-driven analysis can highlight key differences in protocol effectiveness, enabling you to choose the best option for reproducibility and accuracy in your glutamine studies.

Are there different types or variations of glutamine that researchers should be aware of?

Yes, there are sveeral different forms of glutamine that researchers may encounter. The most common forms include L-glutamine, which is the naturally occurring amino acid, and D-glutamine, which is a less common isomer. There are also some specialty glutamine products, such as glutamine peptides or glutamine-rich protein supplements. Each form may have slightly different properties and potential applications, so it's important for researchers to be aware of these variations when designing and evaluating glutamine-related studies.

More about "Glutamine"

Glutamine, a nonessential amino acid, plays a pivotal role in human physiology.
As a precursor for amino acids, proteins, and nucleic acids, glutamine is essential for energy production, acid-base balance, and immune function.
Its importance extends to the gastrointestinal tract, muscle tissue, and the brain, making it crucial for overall wellbeing and healing processes.
Researchers continue to explore the therapeutic potential of glutamine supplementation in various clinical conditions, such as sports performance, critical illness, and neurological disorders.
L-glutamine, the most common form of glutamine, is often used in cell culture media like DMEM and RPMI 1640, along with other supplements like fetal bovine serum (FBS), penicillin, and streptomycin.
Understanding the comprehensive impact of glutamine on the human body is essential for optimizing research protocols and enhancing reproducibility.
Leveraging the power of AI-driven platforms like PubCompare.ai can help researchers identify the most effective protocols and gain data-driven insights, streamlining their glutamine-related investigations.
By incorporating relevant synonyms, abbreviations, and key subtopics, this content aims to provide a thorough and SEO-optimized overview of the physiological importance and research areas surrounding glutamine.