The largest database of trusted experimental protocols

4 protocols using quaternary solvent manager r

1

Molecular Weight Estimation by SEC

Check if the same lab product or an alternative is used in the 5 most similar protocols
Molecular
weights (MWs) were estimated by size exclusion chromatography (SEC)
on an Acquity Arc equipped with a 2998PDA Detector, a Sample Manager
FTN-R, and a Quaternary Solvent Manager-R (Acquity Arc, Waters Corporation,
Milford, MA, USA) with a XBridge TM Protein BEH SEC 200 Å 2.5
μm 4.6 mm × 150 mm column. The standard proteins (Waters
Corporation, Milford, MA, USA) were used to calibrate the column:
uracil (0.112 kDa), ribonuclease A (13.7 kDa), albumin chicken egg
white (44.2 kDa), and thyroglobulin bovine (669 kDa).3 (link) A volume of 10 μL dissolved in 100 mM sodium phosphate
buffer and 0.02% (w/v) sodium azide adjusted at pH 6.8 at a concentration
of 1 mg/mL was injected. Protein elution was recorded by measuring
its absorbance at 280 nm and analyzed with Empower 3 Personal GPC/SEC
software (Waters Corporation, Milford, MA, USA).
+ Open protocol
+ Expand
2

Analytical Characterization of Organic Compounds

Check if the same lab product or an alternative is used in the 5 most similar protocols
1H and 13C{1H} NMR spectra were recorded on a Bruker AVANCE III 400 MHz spectrometer or a Bruker AVANCE III 500 MHz spectrometer in CDCl3. Spectra were referenced internally by using the residual solvent (1H: δ 7.26) or solvent (13C: δ 77.2) resonance relative to SiMe4. ESI mass spectra were recorded on a Thermo Finnigan MAT 95 XL mass spectrometer. Electronic absorption and steady‐state fluorescence spectra were taken on a Cary 5G UV–Vis–NIR spectrophotometer and a HORIBA FluoroMax‐4 spectrofluorometer, respectively. Reverse‐phase HPLC separation was performed on an Apollo‐C18 column (5 µm, 4.6 mm × 150 mm) at a flow rate of 1 mL min−1 for analytical purpose or on a XBridge BEH300 Prep C18 column (5 µm, 10 mm × 250 mm) at a flow rate of 3 mL min−1 for preparative purpose, using a Waters system equipped with a Waters 1525 binary pump and a Waters 2998 photodiode array detector. The solvents used for HPLC analysis were of HPLC grade. LC‐MS studies were performed on a XSelect CSH C18 column (5 µm, 4.6 mm × 250 mm) at a flow rate of 0.8 mL min−1 using a Waters system equipped with a Waters Quaternary Solvent Manager‐R, a Waters 2998 photodiode array detector, a Waters 2475 fluorescence detector, and a Waters single quadrupole detector 2. The solvents used were of LC‐MS grade.
+ Open protocol
+ Expand
3

Chiral Separation of Compound 7

Check if the same lab product or an alternative is used in the 5 most similar protocols
The racemic mixture of 7 was separated by normal phase HPLC. The semi-preparative instrument used was equipped with a 333 pump (Gilson, Villiers-le-Bel, France) and a UV 2487 detector (Waters, USA). PDR-Chiral Inc. software (PDR-Chiral Inc., West Palm Beach, FL, USA) was used for chromatographic data collection. The preparative column used was Chiralcel® OD, with dimensions of 250 × 20 mm and a particle size of 5µm (Chiral Technologies, Illkirch-Graffenstaden, France). A mixture of heptane/ethanol/triethylamine (80/20/0.1 v/v/v) was used as an eluent at a flowrate of 18 mL/min. Each cycle, 25 mg of 7 was injected. The chromatographic peaks were detected at 250 nm.
Collected fraction were analyzed on an Acquity Arc HPLC equipped with a 2998 PDA detector, a Quaternary Solvent Manager—R, and a Column Manager -30S, all from Waters (Waters, USA), using the software Empower® 3 (Waters, USA) for chromatographic data evaluation. The analytical column used was a CelluCoat® 150 × 4.6 mm 3 µm column (Nouryon, Alby, Sweden), with a mixture of heptane/ethanol/trimethylamine (80/20/0.1 v/v/v) as the eluent at a flowrate of 0.8 mL/min. The column temperature was 25 °C, and the chromatographic peaks were detected at 260 nm.
+ Open protocol
+ Expand
4

Amino Acid Composition Analysis by UHPLC

Check if the same lab product or an alternative is used in the 5 most similar protocols
The amino acid content was evaluated according to the method of Alaiz et al. with slight modifications [16 (link)]. The samples were hydrolyzed with HCl at 110 °C for 24 h in tubes sealed under nitrogen. Determination of the amino acid content in the acid hydro-lysate was carried out by ultra-high-performance liquid chromatography in a Acquity Arc equipped with a 2998PDA Detector, a Sample Manager FTN-R and a Quaternary Solvent Manager-R (Acquity Arc, Waters corporation, Milford, MA, USA), after derivatization with diethyl ethoxymethylenemalonate, using D,L-α-aminobutiric acid as the internal standard, and a 3 mm × 150 mm reversed-phase column (XSlect® HSS T3, 2.5 µm) (Waters corporation, Milford, MA, USA). Two solvents: (A) 25-mM sodium acetate and 0.02% sodium azide (pH 6.0) and (B) acetonitrile were used to constitute a binary system gradient. For each amino acid, calibration curves were developed using a mix acid standard at the same hydrolysis conditions of the samples (Merck, Madrid, Spain), and the resultant peaks were detected by measuring its absorbance at 280 nm analyzed with EMPOWER software (Waters, Santa Clara, CA, USA). We used the Yust method to determine the tryptophan content [17 (link)].
+ Open protocol
+ Expand

About PubCompare

Our mission is to provide scientists with the largest repository of trustworthy protocols and intelligent analytical tools, thereby offering them extensive information to design robust protocols aimed at minimizing the risk of failures.

We believe that the most crucial aspect is to grant scientists access to a wide range of reliable sources and new useful tools that surpass human capabilities.

However, we trust in allowing scientists to determine how to construct their own protocols based on this information, as they are the experts in their field.

Ready to get started?

Sign up for free.
Registration takes 20 seconds.
Available from any computer
No download required

Sign up now

Revolutionizing how scientists
search and build protocols!