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Maltose
Maltose
Maltose is a disaccharide composed of two glucose units linked by an alpha-1,4-glycosidic bond.
It is a common byproduct of starch digestion and can be used in a variety of food and industrial applications.
PubCompare.ai's AI-powered platform helps researchers effortlessly locate the best protocols from literature, pre-prints, and patents, enabling data-driven comparisons to optimize maltose-related studies and maximize research outcomes.
Discover how PubCompare.ai can enhance the reproducibility and accuracy of your maltose research and take your studies to new heights.
It is a common byproduct of starch digestion and can be used in a variety of food and industrial applications.
PubCompare.ai's AI-powered platform helps researchers effortlessly locate the best protocols from literature, pre-prints, and patents, enabling data-driven comparisons to optimize maltose-related studies and maximize research outcomes.
Discover how PubCompare.ai can enhance the reproducibility and accuracy of your maltose research and take your studies to new heights.
Most cited protocols related to «Maltose»
Amylose
Buffers
Chloroform
Deoxyribonuclease EcoRI
DNA Chips
DNA Library
Endopeptidase K
Ethanol
Genome
Genome, Mitochondrial
Immunocytochemistry
Immunoglobulins
Maltose
Nucleic Acids
Oligonucleotide Primers
Phenol
Proteins
Ribonuclease H
Ribosomes
Fresh faecal samples were obtained from six consenting healthy adult human donors (1 faecal sample per donor: minimum 0.5 g) and were placed in anaerobic conditions within 1 h of passing to preserve the viability of anaerobic bacteria. All sample processing and culturing took place under anaerobic conditions in a Whitley DG250 workstation at 37 °C. Culture media, PBS and all other materials that were used for culturing were placed in the anaerobic cabinet 24 h before use to reduce to anaerobic conditions. The faecal samples were divided in two. One part was homogenized in reduced PBS (0.1 g stool per ml PBS) and was serially diluted and plated directly onto YCFA7 (link) agar supplemented with 0.002 g ml−1 each of glucose, maltose and cellobiose in large (13.5 cm diameter) Petri dishes. This sample was also subjected to metagenomic sequencing to profile the entire community. The other part was treated with an equal volume of 70% (v/v) ethanol for 4 h at room temperature under ambient aerobic conditions to kill vegetative cells. Then, the solid material was washed three times with PBS and it was eventually resuspended in PBS. Plating was performed as described earlier.
For the ethanol-treated samples, the medium was supplemented with 0.1% sodium taurocholate to stimulate spore germination. Colonies were picked 72 h after plating from Petri dishes of both ethanol-treated and non-ethanol-treated conditions harbouring non-confluent growth, (that is, plates on which the colonies were distinct and not touching). The colonies that were picked were re-streaked to confirm purity. No statistical methods were used to predetermine sample size. The experiments were not randomized. The investigators were not blinded to allocation during experiments and outcome assessment.
For the ethanol-treated samples, the medium was supplemented with 0.1% sodium taurocholate to stimulate spore germination. Colonies were picked 72 h after plating from Petri dishes of both ethanol-treated and non-ethanol-treated conditions harbouring non-confluent growth, (that is, plates on which the colonies were distinct and not touching). The colonies that were picked were re-streaked to confirm purity. No statistical methods were used to predetermine sample size. The experiments were not randomized. The investigators were not blinded to allocation during experiments and outcome assessment.
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Adult
Agar
Bacteria, Aerobic
Bacterial Viability
Cellobiose
Cells
Donors
Ethanol
Feces
Germination
Glucose
Hyperostosis, Diffuse Idiopathic Skeletal
Maltose
Metagenome
Spores
Taurocholic Acid, Monosodium Salt
Tissue Donors
All of the C. albicans strains used in this study were derived from strain SC5314, and a complete list of the strains is provided in Table S2 . nourseothricin-sensitive C. albicans strains were cultured in yeast extract-peptone-dextrose (YPD) liquid medium at 30°C and harvested at an optical density at 600 nm between 0.5 and 0.8 prior to transformation by a modified version of the standard lithium acetate protocol (10 ); see our detailed protocol in Text S1 . After recovery in liquid YPD for 5 h, nourseothricin-resistant transformants were selected on YPD agar supplemented with 200 µg/ml nourseothricin (GoldBio). Subsequent removal of the CRISPR components was performed by single-colony isolation on synthetic defined (SD) agar medium minus leucine for the LEUpOUT method or by culturing overnight in YP-maltose liquid medium, followed by screening on YPD agar supplemented with 25 µg/ml nourseothricin for the FLP recombinase-mediated method (see Text S1 for details). The generation of homozygous URA3 deletion strains was confirmed by patching to SD minus uracil versus YPD plates; both medium types were supplemented with 200 µg/ml nourseothricin to maintain selection for strains that had integrated the CRISPR components. All E. coli strains were derived from DH5α and cultured at 37°C in LB medium supplemented with 100 µg/ml carbenicillin.
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Agar
Carbenicillin
Clustered Regularly Interspaced Short Palindromic Repeats
Culture Media
Deletion Mutation
Escherichia coli
FLP recombinase
Glucose
Homozygote
isolation
Leucine
lithium acetate
Maltose
Nourseothricin
Peptones
Strains
Uracil
Yeasts
Radiolabeled β-catenin (5 μl) was phosphorylated using 300 nM His-tagged GSK3β and 100 nM maltose-binding protein (MBP)–axin in 20 μl of XB containing 10 mM ATP, 20 mM MgSO4, and 50 mM NaCl. For the nonphorphorylated control, β-catenin was incubated as above, except that 50 mM LiCl was used instead of NaCl to inhibit GSK3β. The kinase reactions were incubated in a shaker for 30 min at 20°C and then added to 50 μl of MBP–axin, bound to amylose beads (1 mg of protein per milliliter of beads), and brought up to 250 μl with XB containing 50 mM LiCl. After phorsphorylated and nonphosphorylated β-catenin, respectively, bound to axin beads, the beads were washed three times with 500 μl of XB containing 50 mM LiCl. Dissociation of the bound β-catenin was initiated by adding 1 μM unlabeled recombinant β-catenin (His-tagged, from Sf9 cells) and incubated at 20°C in a shaker. At the appropriate times, 5 μl aliquots of beads were quickly removed, filtered through Wizard minicolumns (Promega, Madison, Wisconsin, United States), and washed with ice-cold XB (3 ml). Proteins bound to beads were eluted from the minicolumns with 20 μl of hot sample buffer, followed by SDS-PAGE and autoradiography.
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Amylose
Autoradiography
Axin Protein
Buffers
Cardiac Arrest
Cold Temperature
CTNNB1 protein, human
GSK3B protein, human
Maltose
Maltose-Binding Proteins
Phosphotransferases
Promega
Proteins
SDS-PAGE
Sf9 Cells
Sodium Chloride
Sulfate, Magnesium
Human β2AR fused to an amino-terminal T4 lysozyme23 (link) was expressed and purified as described above. Following purification by alprenolol sepharose, the receptor was washed extensively with 30 μM of the low affinity antagonist atenolol while bound to FLAG affinity resin to fully displace alprenolol, then washed and eluted in buffer devoid of ligand to produce a homogeneously unliganded preparation. The receptor was then incubated for 30 minutes at room temperature with a stoichiometric excess of ligand (HBI or BI167107). A 1.3-fold molar excess of Nb6B9 was then added, and the sample was dialyzed overnight into a buffer consisting of 100 mM sodium chloride, 20 mM HEPES pH 7.5, 0.01% lauryl maltose neopentyl glycol detergent, and 0.001% cholesteryl hemisuccinate. In each case, ligand was included in the dialysis buffer at 100 nM concentration or higher. The sample was then concentrated using a 50 kDa spin concentrator and purified over a Sephadex S200 size exclusion column in the same buffer as for dialysis, and the β2AR-Nb6B9-ligand ternary complex was isolated. In the case of adrenaline, the low affinity and chemical instability of the ligand precluded overnight dialysis, so 100 μM adrenaline was added to receptor for 30 minutes at room temperature, then a 1.3-fold molar excess of Nb6B9 added and the sample was incubated for 30 minutes at room temperature. Following incubation, the sample was concentrated and immediately purified by size exclusion as above.
Following purification, samples were concentrated to A280 = 55 using a 50 kDa concentrator to minimize the detergent concentration in the final sample, then aliquoted into thin-walled PCR tubes at 8 μL per aliquot. Aliquots were flash frozen in liquid nitrogen and stored at -80 °C for crystallization trials. For crystallization, samples were thawed and reconstituted into lipidic cubic phase with a 1:1 mass:mass ratio of lipid. The lipid stock consisted of a 10:1 mix by mass of 7.7 monoacylglycerol (generously provided by Martin Caffrey) with cholesterol (Sigma). Samples were reconstituted by the two syringe mixing method10 (link) and then dispensed into glass sandwich plates using a GryphonLCP robot (Art Robbins Instruments). In the case of the β2AR-adrenaline complex, 1 mM fresh adrenaline was mixed with receptor prior to reconstitution. Crystals were grown using 30 nL protein/lipid drops with 600 nL overlay solution, which consisted of 18 – 24 % PEG400, 100 mM MES pH 6.2 to pH 6.7, and 40 – 100 mM ammonium phosphate dibasic. Crystals grew in 1 – 3 days, and were harvested and frozen in liquid nitrogen for data collection.
Following purification, samples were concentrated to A280 = 55 using a 50 kDa concentrator to minimize the detergent concentration in the final sample, then aliquoted into thin-walled PCR tubes at 8 μL per aliquot. Aliquots were flash frozen in liquid nitrogen and stored at -80 °C for crystallization trials. For crystallization, samples were thawed and reconstituted into lipidic cubic phase with a 1:1 mass:mass ratio of lipid. The lipid stock consisted of a 10:1 mix by mass of 7.7 monoacylglycerol (generously provided by Martin Caffrey) with cholesterol (Sigma). Samples were reconstituted by the two syringe mixing method10 (link) and then dispensed into glass sandwich plates using a GryphonLCP robot (Art Robbins Instruments). In the case of the β2AR-adrenaline complex, 1 mM fresh adrenaline was mixed with receptor prior to reconstitution. Crystals were grown using 30 nL protein/lipid drops with 600 nL overlay solution, which consisted of 18 – 24 % PEG400, 100 mM MES pH 6.2 to pH 6.7, and 40 – 100 mM ammonium phosphate dibasic. Crystals grew in 1 – 3 days, and were harvested and frozen in liquid nitrogen for data collection.
Alprenolol
ammonium phosphate
Atenolol
BI167107
Buffers
Cholesterol
cholesterol-hemisuccinate
Crystallization
Cuboid Bone
Detergents
Dialysis
Epinephrine
Freezing
Glycols
HEPES
Homo sapiens
Ligands
Lipids
Maltose
Molar
Monoglycerides
Nitrogen
polyethylene glycol 400
Proteins
Resins, Plant
sephadex
Sepharose
Sodium Chloride
Syringes
Most recents protocols related to «Maltose»
Example 14
Six formulations including alkalized cocoa powder were tested in a vacuum expanded hard candy beverage enhancer. All formulations had the same amounts of sucrose, high-maltose (HM) corn syrup, and stevia, as shown in Table 3. The amounts of water and alkalized cocoa powder or chocolate flavoring varied. For each formulation, all of the ingredients in Table 3 except for the stevia were mixed and cooked on a stovetop to about 295° F. (about 146° C.). The stevia was then added while gradually decreasing the temperature. The resulting hard candy was pulled for 15 seconds; Formulas A-E were mechanically pulled and Formula F was manually pulled. A drop roller was used to created spherical pieces of the hard candy. The spherical pieces were then vacuum-expanded in an oven. For the vacuum expansion, the candy was placed on pans lined with crumpled aluminum foil and was heated and expanded for about 10 minutes at an oven temperature of about 155° F. (about 68° C.). The disintegration times in Table 3 are for disintegration in milk at a refrigerated temperature of about 40° F. to about 32° F. (about 4° C. to about 0° C.).
While the foregoing specification illustrates and describes exemplary embodiments, it will be understood by those skilled in the art that various changes may be made and equivalents may be substituted for elements thereof without departing from the scope of the invention. In addition, many modifications may be made to adapt a particular situation or material to the teachings of the invention without departing from the essential scope thereof. Therefore, it is intended that the invention not be limited to the particular embodiment disclosed as the best mode contemplated for carrying out this invention, but that the invention will include all embodiments falling within the scope of the appended claims.
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Aluminum
Beverages
Candy
Chocolate
Cocoa Powder
Corns
Maltose
Milk, Cow's
Neoplasm Metastasis
Stevia
Sucrose
Vacuum
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Bacteria
Buffers
Cells
Centrifugation
Chromatography
Escherichia coli
Glutathione
imidazole
Isopropyl Thiogalactoside
Maltose
Neoplasm Metastasis
Nonidet P-40
Plasmids
Proteins
SDS-PAGE
Sepharose
Sodium Chloride
Strains
Tromethamine
Vision
Baculoviruses were prepared using the Bac-to-Bac Baculovirus Expression System (Thermo Fisher). Sf9 insect cells were cultured to a density of 3 × 106 cells per mL and co-infected with FLAG-His 8-ETAR(21–406)/ETBR(27–424)-LgBiT, engineered Gαq/Gαi, Gβ1-15AA-HiBiT, Gγ2, and scFv16 baculoviruses at a 1:1:1:1:1 ratio. The cells were then harvested by centrifugation 48 h post-infection and stored at −80 °C for future use.
The frozen cells were thawed on ice and resuspended in lysis buffer containing 20 mM HEPES, pH 7.5, 100 mM NaCl, 10% (v/v) glycerol, 10 mM MgCl2, 5 mM CaCl2, and supplemented with EDTA-free protease inhibitor cocktail (TargetMol). For ET-1-ETAR-Gq/ IRL1620-ETBR-Gi complex, cells were lysed by dounce homogenization and complex formation was initiated with the addition of 25 mU/mL Apyrase (Sigma-Aldrich) and 10 μM ET-1/ IRL1620 (GenScript) for 1.5 h at room temperature (RT). The membrane was then solubilized by adding 0.5% (w/v) lauryl maltose neopentyl glycol (LMNG, Anatrace) and 0.1% (w/v) cholesterol hemisuccinate (CHS, Anatrace) for 2 h at 4 °C. The sample was clarified by centrifugation at 80,000×g for 30 min and the supernatant was then incubated with anti-DYKDDDDK Affinity Beads (GenScript) for 3 h at 4 °C. After incubation, the resin was collected by centrifugation (600×g, 10 min) and loaded into a gravity flow column, followed by a wash with 20-column volumes of 20 mM HEPES, pH 7.5, 100 mM NaCl, 10% (v/v) glycerol, 5 mM MgCl2, 1 μM ET-1/IRL1620, 0.01% (w/v) LMNG, and 0.002% (w/v) CHS. The protein was finally eluted with ten-column volumes of 20 mM HEPES, pH 7.5, 100 mM NaCl, 10% (v/v) glycerol, 5 mM MgCl2, 1 μM ET-1/IRL1620, 0.01% (w/v) LMNG, and 0.2 mg/mL FLAG peptide. The purified complexes were concentrated using an Amicon Ultra centrifugal filter (molecular weight cut-off of 100 kDa, Millipore) and then subjected to a Superose 6 Increase 10/300 GL column (GE Healthcare) that was pre-equilibrated with buffer containing 20 mM HEPES, pH 7.5, 100 mM NaCl, 2 mM MgCl2, 1 μM ET-1/IRL1620, 0.00075% (w/v) LMNG, 0.00025% (w/v) GDN, and 0.0002% (w/v) CHS. The purification procedure of ET-1-ETBR-Gq complex was similar to ETAR, expect the addition of 0.05% (w/v) digitonin, the final size-column equilibrated with 0.05% (w/v) digitonin instead of 0.00075% (w/v) LMNG, 0.00025% (w/v) GDN, and 0.0002% (w/v) CHS. The monomeric fractions of the complex were collected and concentrated for cryo-EM examination.
The frozen cells were thawed on ice and resuspended in lysis buffer containing 20 mM HEPES, pH 7.5, 100 mM NaCl, 10% (v/v) glycerol, 10 mM MgCl2, 5 mM CaCl2, and supplemented with EDTA-free protease inhibitor cocktail (TargetMol). For ET-1-ETAR-Gq/ IRL1620-ETBR-Gi complex, cells were lysed by dounce homogenization and complex formation was initiated with the addition of 25 mU/mL Apyrase (Sigma-Aldrich) and 10 μM ET-1/ IRL1620 (GenScript) for 1.5 h at room temperature (RT). The membrane was then solubilized by adding 0.5% (w/v) lauryl maltose neopentyl glycol (LMNG, Anatrace) and 0.1% (w/v) cholesterol hemisuccinate (CHS, Anatrace) for 2 h at 4 °C. The sample was clarified by centrifugation at 80,000×g for 30 min and the supernatant was then incubated with anti-DYKDDDDK Affinity Beads (GenScript) for 3 h at 4 °C. After incubation, the resin was collected by centrifugation (600×g, 10 min) and loaded into a gravity flow column, followed by a wash with 20-column volumes of 20 mM HEPES, pH 7.5, 100 mM NaCl, 10% (v/v) glycerol, 5 mM MgCl2, 1 μM ET-1/IRL1620, 0.01% (w/v) LMNG, and 0.002% (w/v) CHS. The protein was finally eluted with ten-column volumes of 20 mM HEPES, pH 7.5, 100 mM NaCl, 10% (v/v) glycerol, 5 mM MgCl2, 1 μM ET-1/IRL1620, 0.01% (w/v) LMNG, and 0.2 mg/mL FLAG peptide. The purified complexes were concentrated using an Amicon Ultra centrifugal filter (molecular weight cut-off of 100 kDa, Millipore) and then subjected to a Superose 6 Increase 10/300 GL column (GE Healthcare) that was pre-equilibrated with buffer containing 20 mM HEPES, pH 7.5, 100 mM NaCl, 2 mM MgCl2, 1 μM ET-1/IRL1620, 0.00075% (w/v) LMNG, 0.00025% (w/v) GDN, and 0.0002% (w/v) CHS. The purification procedure of ET-1-ETBR-Gq complex was similar to ETAR, expect the addition of 0.05% (w/v) digitonin, the final size-column equilibrated with 0.05% (w/v) digitonin instead of 0.00075% (w/v) LMNG, 0.00025% (w/v) GDN, and 0.0002% (w/v) CHS. The monomeric fractions of the complex were collected and concentrated for cryo-EM examination.
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Apyrase
Baculoviridae
Buffers
Cells
Centrifugation
cholesterol-hemisuccinate
Cultured Cells
Digitonin
Edetic Acid
EDNRB protein, human
FLAG peptide
Freezing
Glycerin
Glycols
Gravity
HEPES
Infection
Insecta
Magnesium Chloride
Maltose
Protease Inhibitors
Proteins
Resins, Plant
Sf9 Cells
Sodium Chloride
Tissue, Membrane
The NavAb cDNA carrying N49K mutation was kindly provided by Dr Katsumasa Irie of Nagoya University, Japan (28 (link)). The cDNA-encoding NavAb channel carrying N49K/T206A mutation was subcloned into the pET28 vector to express monomeric NavAb channels. The NavAb tandem tetramer was constructed by linking four NavAb cDNAs (N49K) with flexible linkers containing 2xGGGS and ‘LVPRGS’ thrombin-cutting sites between each subunit. The NavAb proteins were expressed in E. coli KRX host cells, and cell cultures were induced when A600 reached 0.6, by 0.1 mM isopropyl β-D-1-thiogalactopyranoside and 0.1% L-rhamnose (w/v) overnight under 25 °C. The cells were harvested and resuspended into the resuspension buffer containing 20 mM Tris–HCl, 150 mM NaCl, proteinase inhibitor cocktail (2 mM phenylmethylsulfonyl fluoride, 1 mM AEBSF, 1.5 μM Pepstatin, 1.4 μM E−64, 4 μM Bestatin), DNase I, pH 8.0, then homogenized by a Microfluidizer (Microfluidics Inc). The membranes were collected by ultracentrifugation under 4 °C, 100,000g for 3 h, then resuspended into the resuspension buffer with an additional 20 mM imidazole. The NavAb proteins were extracted from membranes by 1% (w/v) lauryl maltose neopentyl glycol (LMNG), under 4 °C for 3 h and then purified by Talon cobalt resin (Takara Inc) (23 , 28 (link)). The affinity-purified NavAb proteins were further separated by a Superdex 200 size-exclusion column using the gel filtration buffer containing 20 mM Tris, 150 mM NaCl, 0.1% LMNG, pH 8.0. The tetramer fractions of NavAb proteins were pooled and concentrated by Amicon ultrafilters. The NavAb T36C/Q115C mutant proteins for smFRET studies were bound to Talon cobalt resin and then changed into the fluorophore-labeling buffer containing 20 mM Tris, 150 mM NaCl, 0.1% LMNG, pH 7.0. The NavAb proteins bound to cobalt resin were incubated with 100 μM Cy3/Cy5 c5 maleimide (1:1) with improved photostabilities (29 ) at 4 °C for 2 h. The free fluorophores were removed by the gel filtration buffer containing 20 mM imidazole and then eluted by the gel filtration buffer containing 500 mM imidazole. The fluorophore-labeled NavAb tetramer proteins were further separated by a Superdex 200 column and then either reconstituted immediately or stored in a −80 °C freezer. The human voltage-gated proton channel hHv1 was expressed, purified, labeled, and reconstituted as described previously (23 , 24 ).
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4-(2-aminoethyl)benzenesulfonylfluoride
Buffers
Cell Culture Techniques
Cells
Claw
Cloning Vectors
Cobalt
Deoxyribonuclease I
DNA, Complementary
Escherichia coli
Gel Chromatography
Glycols
Homo sapiens
Human Herpesvirus 1
imidazole
maleimide
Maltose
Mutant Proteins
Mutation
pepstatin
Phenylmethylsulfonyl Fluoride
Protease Inhibitors
Proteins
Protein Subunits
Protons
Resins, Plant
Rhamnose
Sodium Chloride
Tetrameres
Thrombin
Tissue, Membrane
Tromethamine
ubenimex
Ultracentrifugation
NPRE were collected, lyophilized, and the dry material (50 mg) was extracted using 1.2 ml of methanol by vortexing 1 minute and then sonicated at room temperature for 20 min. After centrifugation, 500 µL of the supernatant was transferred into two centrifuge tubes for measurement of sugars and acids. For sugars, 20 µL of 3 mg/ml phenyl-β-D-glucopyranoside and 20 µL of 0.1 mg/ml 3-(4-hydroxyphenyl)-propionic acid were added as internal standards. The derivatization of sugars was performed by adding 120 μL methoxyamine-hydrochloride (20 mg/ml in pyridine) for 60 min at 30°C and with 120 μL N,O-bis (trimethylsilyl) trifluoro-acetamide (BSTFA) for 120 min at 45°C, 700 rpm. For amino acids and organic acids, 20 µL of 0.1 mg/ml 3-(4-hydroxyphenyl)-propionic acid was added to the sample as the internal standard and the derivatization was performed by adding 120 µL of methoxylamin-hydrochloride (20 mg/ml in pyridine) for 90 min at 37°C, 700 rpm, followed by addition of 120µl of dimethyl-tert-butylsilyl (TBDMS) and incubated for 30 min at 60°C, 700 rpm. After centrifuging, 100 µL of the supernatant was transferred to vials for detection using TSQ Duo GC-MS/MS (Thermo Fisher Scientific).
Based on NPRE composition, medium mimicking peanut root exudates (MMPRE) was recomposed as follows: Maltose 1.09 g/l; Glucose 0.88 g/l; Arabinose 0.67 g/l; Fructose 0.28 g/l; Trehalose 0.14 g/l; Myo-inositol 0.07 g/l; Lactic acid 2.73 g/l; Succinic acid 0.13 g/l; Malonic acid 0.11 g/l; Fumaric acid 0.07 g/l; Pyruvic acid 0.03 g/l; Pyroglutamic acid 0.02 g/l; Malic acid 0.02 g/l; Citric acid 0.02 g/l; Valine 1.05 g/l; Leucine 0.57 g/l; Threonine 0.57 g/l; Isoleucine 0.42 g/l; Alanine 0.32 g/l; Phenylalanine 0.32 g/l; Tyrosine 0.15 g/l; Serine 0.14 g/l; Glycine 0.11 g/l; Asparagine 0.08 g/l; Glutamic acid 0.03 g/l. Salt and micronutrients were added with these proportions: 0.25 g/l MgSO4·7H2O; 0.34 g/l; K2HPO4; 3-morpholino-1-propanesulfonic acid MOPS 10.5 g/l; 0.25 g/l KCl, 1 g/l (NH4)2SO4; 1.2 mg/l Fe2(SO4)3; 0.4 mg/l MnSO4; 1.6 mg/l CuSO4, 4 mg/l Na2 MoO4, pH adjusted to 7. In case of assay on solid MMPRE, 20 g/l of agar was used for this preparation.
Based on NPRE composition, medium mimicking peanut root exudates (MMPRE) was recomposed as follows: Maltose 1.09 g/l; Glucose 0.88 g/l; Arabinose 0.67 g/l; Fructose 0.28 g/l; Trehalose 0.14 g/l; Myo-inositol 0.07 g/l; Lactic acid 2.73 g/l; Succinic acid 0.13 g/l; Malonic acid 0.11 g/l; Fumaric acid 0.07 g/l; Pyruvic acid 0.03 g/l; Pyroglutamic acid 0.02 g/l; Malic acid 0.02 g/l; Citric acid 0.02 g/l; Valine 1.05 g/l; Leucine 0.57 g/l; Threonine 0.57 g/l; Isoleucine 0.42 g/l; Alanine 0.32 g/l; Phenylalanine 0.32 g/l; Tyrosine 0.15 g/l; Serine 0.14 g/l; Glycine 0.11 g/l; Asparagine 0.08 g/l; Glutamic acid 0.03 g/l. Salt and micronutrients were added with these proportions: 0.25 g/l MgSO4·7H2O; 0.34 g/l; K2HPO4; 3-morpholino-1-propanesulfonic acid MOPS 10.5 g/l; 0.25 g/l KCl, 1 g/l (NH4)2SO4; 1.2 mg/l Fe2(SO4)3; 0.4 mg/l MnSO4; 1.6 mg/l CuSO4, 4 mg/l Na2 MoO4, pH adjusted to 7. In case of assay on solid MMPRE, 20 g/l of agar was used for this preparation.
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acetamide
Acids
Agar
Alanine
Amino Acids
Arabinose
Arachis hypogaea
Asparagine
Biological Assay
Centrifugation
Citric Acid
Exudate
Fructose
fumaric acid
Gas Chromatography-Mass Spectrometry
Glucose
Glutamic Acid
Glycine
Inositol
Isoleucine
Lactic Acid
Leucine
malic acid
malonic acid
Maltose
Methanol
methoxyamine hydrochloride
Micronutrients
Morpholinos
N,N-bis(trimethylsilyl)-2,2,2-trifluoroacetamide
Phenylalanine
phloretic acid
Plant Roots
potassium phosphate, dibasic
pyridine
Pyrrolidonecarboxylic Acid
Pyruvic Acid
SAMHD1 protein, human
Serine
Sodium Chloride
Succinic Acid
Sugars
Sulfate, Magnesium
TERT protein, human
Threonine
Trehalose
Tyrosine
Valine
Top products related to «Maltose»
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Maltose is a disaccharide composed of two glucose units linked together. It is commonly used as a standard in various biochemical and analytical laboratory applications to measure the activity or concentration of enzymes, such as amylases, that cleave maltose into glucose units.
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Amylose resin is a chromatography resin used for the purification of proteins and enzymes. It functions by selectively binding to proteins with a high affinity for amylose, a component of starch. This resin can be used to isolate and concentrate target proteins from complex mixtures.
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Sucrose is a disaccharide composed of glucose and fructose. It is commonly used as a laboratory reagent for various applications, serving as a standard reference substance and control material in analytical procedures.
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Fructose is a type of monosaccharide sugar that is commonly used in laboratory settings. It is a naturally occurring carbohydrate found in fruits, honey, and certain vegetables. Fructose serves as a key component in various experimental and analytical procedures, particularly in the fields of biochemistry, food science, and nutrition research.
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Lactose is a disaccharide sugar composed of galactose and glucose. It is a key component in the regulation of gene expression and the maintenance of cellular metabolism. Lactose is commonly used in various laboratory applications, including cell culture, enzymatic assays, and biochemical analyses.
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D-glucose is a type of monosaccharide, a simple sugar that serves as the primary source of energy for many organisms. It is a colorless, crystalline solid that is soluble in water and other polar solvents. D-glucose is a naturally occurring compound and is a key component of various biological processes.
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Galactose is a monosaccharide that serves as a core component in various laboratory analyses and experiments. It functions as a fundamental building block for complex carbohydrates and is utilized in the study of metabolic processes and cellular structures.
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Sodium hydroxide is a chemical compound with the formula NaOH. It is a white, odorless, crystalline solid that is highly soluble in water and is a strong base. It is commonly used in various laboratory applications as a reagent.
Sourced in United States, Germany, Italy, Belgium, China, United Kingdom, Sao Tome and Principe, India
D-fructose is a monosaccharide that can be used as a laboratory reagent. It is a natural sugar found in fruits and honey. D-fructose has the molecular formula C6H12O6 and serves as a fundamental building block for carbohydrates.
More about "Maltose"
Maltose, a disaccharide composed of two glucose units linked by an alpha-1,4-glycosidic bond, is a common byproduct of starch digestion.
This versatile carbohydrate finds applications in a variety of food and industrial processes.
Closely related to other sugars like sucrose, fructose, and lactose, maltose shares some structural and functional similarities, while also maintaining its own unique properties.
Amylose resin, a key component in the purification of maltose, plays a crucial role in the extraction and refinement of this important sugar.
D-glucose and galactose, as monosaccharides, are the building blocks of maltose and other disaccharides, highlighting the interconnected nature of carbohydrate chemistry.
Sodium hydroxide, a common chemical reagent, can be utilized in the processing and modification of maltose, enabling the tailoring of its characteristics for specific applications.
Maltose's ability to be broken down into its constituent glucose units, a process known as hydrolysis, makes it a valuable intermediate in the production of other valuable sugars and sweeteners.
PubCompare.ai's AI-powered platform empowers researchers to explore the vast landscape of maltose-related studies, helping them effortlessly locate the best protocols from literature, pre-prints, and patents.
This data-driven approach enables informed decision-making and maximizes the accuracy and reproducibility of maltose research, taking studies to new heights and unlocking the full potential of this versatile carbohydrate.
This versatile carbohydrate finds applications in a variety of food and industrial processes.
Closely related to other sugars like sucrose, fructose, and lactose, maltose shares some structural and functional similarities, while also maintaining its own unique properties.
Amylose resin, a key component in the purification of maltose, plays a crucial role in the extraction and refinement of this important sugar.
D-glucose and galactose, as monosaccharides, are the building blocks of maltose and other disaccharides, highlighting the interconnected nature of carbohydrate chemistry.
Sodium hydroxide, a common chemical reagent, can be utilized in the processing and modification of maltose, enabling the tailoring of its characteristics for specific applications.
Maltose's ability to be broken down into its constituent glucose units, a process known as hydrolysis, makes it a valuable intermediate in the production of other valuable sugars and sweeteners.
PubCompare.ai's AI-powered platform empowers researchers to explore the vast landscape of maltose-related studies, helping them effortlessly locate the best protocols from literature, pre-prints, and patents.
This data-driven approach enables informed decision-making and maximizes the accuracy and reproducibility of maltose research, taking studies to new heights and unlocking the full potential of this versatile carbohydrate.