All solvents used for solid phase extraction and HPLC-DAD analyses were LC-MS grade from either Sigma-Aldrich (Madrid, Spain) or VWR Chemicals (Barcelona, Spain). Restriction enzymes and T4 DNA ligase were purchased from Thermo Scientific (Madrid, Spain). p-Coumaric acid, L-phenylalanine and sodium malonate were purchased from Sigma-Aldrich (Madrid, Spain), L-tyrosine from Acros Organics (Thermo Fisher, Madrid, Spain), and cerulenin from Cayman Chemicals (Ann Arbor, Michigan, USA).
L tyrosine
Manufactured by Thermo Fisher Scientific
Sourced in Spain, Germany
L-tyrosine is a non-essential amino acid that plays a crucial role in protein synthesis and various metabolic processes. It serves as a building block for proteins and is involved in the production of neurotransmitters and hormones. As a lab equipment product, L-tyrosine can be used for research and analysis purposes in various scientific fields.
Automatically generated - may contain errors
Lab products found in correlation
T4 dna ligase, by Thermo Fisher Scientific (2 mentions)
Dulbecco phosphate buffered saline (dpbs), by Thermo Fisher Scientific (2 mentions)
Cerulenin, by Cayman Chemical (1 mentions)
Sodium malonate, by Merck Group (1 mentions)
L phenylalanine, by Merck Group (1 mentions)
Lc ms grade, by Merck Group (1 mentions)
Restriction enzyme, by Thermo Fisher Scientific (1 mentions)
P coumaric acid, by Merck Group (1 mentions)
L tryptophan, by Thermo Fisher Scientific (1 mentions)
L phenylalanine, by Thermo Fisher Scientific (1 mentions)
4 protocols using l tyrosine
1
Analytical Procedures for Chemical Extraction
2
Protein Expression and Purification
3
Amino Acid-Enriched Fish Feed Formulation
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Commercial fish feed (L2 Alterna® Skretting, Burgos, Spain), with a size of 2.2 mm, was used as the control diet. L -phenylalanine and L -tyrosine (dry powder) were purchased from ThermoFisher (Kandel, Germany). The commercial control diet was finely ground and mixed with AA and later water (300 mL Kg–1 dry feed). The amount of phenylalanine and tyrosine in each experimental diet was 5% (on dry feed) except for the control diet which did not have any amino acid. The mixture was thread pelleted into 2 mm diameter and 20–25 cm length strips. These were cut to get 2–3 mm size pellets. Finally, these food strips were dried at 30°C for 48 h and stored at 4°C.
Analysis of AA was performed as reported previously (Herrera et al., 2020 (link); Salamanca et al., 2020 (link)). According to the above method, the final amino acid concentrations in the experimental diets are shown inTable 1 .
Analysis of AA was performed as reported previously (Herrera et al., 2020 (link); Salamanca et al., 2020 (link)). According to the above method, the final amino acid concentrations in the experimental diets are shown in
4
Tyrosine and Calmodulin TRAST Measurements
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A stock solution of 160 µM of L-tyrosine in DPBS (ThermoFisher Scientific) was freshly prepared and further diluted to 20 µM for the TRAST measurements, with pH set to 7, or as stated in the text. All chemicals were purchased from Sigma Aldrich, if not stated otherwise. Deoxygenation experiments were performed in a sealed container, where the solution was bubbled with nitrogen gas for twenty minutes before measurements. During the experiment, a low flow of nitrogen was applied over the sample to avoid re-oxygenation.
Calmodulin (CaM, purified from bovine brain Lyophilized from 30 mM HEPES, 1 mM CaCl2, 0.1 mM DTT, pH 7.4), reconstituted to a stock concentration of 1.858 mg/mL, was subsequently diluted to 20 μM for measurements in 30 mM HEPES (pH 7.4). The 20 μM CaM solution was considered calcium-saturated (hereinafter denoted CaM-Ca2+), given that it was expected to contain approximately 180 μM Ca2+, as indicated by the provided lyophilization information from the supplier (Sigma Aldrich). To obtain a calcium-free calmodulin solution (hereinafter denoted CaM-w/o-Ca2+), an excess of EGTA (Ethyleneglycol- bis(β-aminoethyl)-N,N,Nʹ,Nʹ-tetraacetic Acid) was introduced to chelate all calcium ions, while approximately 200 μM of free EGTA remained in the solution.
Calmodulin (CaM, purified from bovine brain Lyophilized from 30 mM HEPES, 1 mM CaCl2, 0.1 mM DTT, pH 7.4), reconstituted to a stock concentration of 1.858 mg/mL, was subsequently diluted to 20 μM for measurements in 30 mM HEPES (pH 7.4). The 20 μM CaM solution was considered calcium-saturated (hereinafter denoted CaM-Ca2+), given that it was expected to contain approximately 180 μM Ca2+, as indicated by the provided lyophilization information from the supplier (Sigma Aldrich). To obtain a calcium-free calmodulin solution (hereinafter denoted CaM-w/o-Ca2+), an excess of EGTA (Ethyleneglycol- bis(β-aminoethyl)-N,N,Nʹ,Nʹ-tetraacetic Acid) was introduced to chelate all calcium ions, while approximately 200 μM of free EGTA remained in the solution.
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