Mercury400 mhz

Manufactured by Bruker

Sourced in United States

The Mercury400 MHz is a nuclear magnetic resonance (NMR) spectrometer designed by Bruker. It operates at a frequency of 400 MHz and is used for the analysis and characterization of chemical compounds.

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Lab products found in correlation

Avance 3 500 mhz spectrometer, by Bruker (3 mentions) Alliance 2695 module, by Waters Corporation (2 mentions) Microtof mass spectrometer, by Bruker (2 mentions) 2996 photodiode array detector, by Phenomenex (1 mentions) Synergi 4μ max rp 80a column, by Phenomenex (1 mentions) 2996 photodiode array detector, by Waters Corporation (1 mentions) Alliance 2695, by Waters Corporation (1 mentions) 2996 pda detector, by Waters Corporation (1 mentions) Nmr tube, by Wilmad (1 mentions) Ph paper, by Merck Group (1 mentions) Drx 500 mhz spectrometer, by Bruker (1 mentions) Ph meter, by Mettler Toledo (1 mentions)

4 protocols using mercury400 mhz

Analytical Characterization of Synthetic Phosphates

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All reagents and solvents were of commercial
quality and were used without further purification, unless described
otherwise. Unless otherwise stated, all reactions were carried out
under an inert atmosphere of argon. ¹H, ¹³C,
and ³¹P NMR spectra were collected on a Varian Mercury
400 MHz or Bruker Avance III 500 MHz spectrometer. All ¹H and ¹³C NMR assignments are based on gCOSY, gHMBC, gHSQC,
and DEPT-135 experiments. Abbreviations for splitting patterns are
as follows: b, broad; s, singlet; d, doublet; t, triplet; m, multiplet.
Coupling constants are given in hertz (Hz). High resolution time-of-flight
mass spectra were obtained on a Bruker Daltonics micrOTOF mass spectrometer
using electrospray ionization (ESI). The purity of new tested compounds
was determined to be ≥95% by analytical HPLC. Analytical HPLC
analyses were carried out on a Waters 2695 Alliance module equipped
with a Waters 2996 photodiode array detector (210–350 nm).
The chromatographic system consisted of a Hichrom Guard column for
HPLC and a Phenomenex Synergi 4 μm MAX-RP 80A column (150 mm
× 4.60 mm), with elution at 1 mL/min with the following ion-pair
buffer: 0.17% (m/v) cetrimide and 45% (v/v) phosphate buffer (pH 6.4)
in MeOH. Synthetic phosphates were assayed and quantified by the Ames
phosphate test.^{57 (link)}

Swarbrick J.M., Graeff R., Zhang H., Thomas M.P., Hao Q, & Potter B.V. (2014). Cyclic Adenosine 5′-Diphosphate Ribose Analogs without a “Southern” Ribose Inhibit ADP-ribosyl Cyclase–Hydrolase CD38. Journal of Medicinal Chemistry, 57(20), 8517-8529.

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Purification and Characterization of Human CD38 Catalytic Domain

Cited 1 time

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All reagents and solvents were of commercial quality and were used without further purification, unless described otherwise. The human CD38 catalytic domain (shCD38) was expressed and purified as described previously^{36 (link),39 (link)}. Unless otherwise stated, all reactions were carried out under an inert atmosphere of argon. ¹H, ¹³C, and ³¹P NMR spectra were collected on a Jeol Delta 270 MHz, Varian Mercury 400 MHz or Bruker Avance III 500 MHz Spectrometer. All ¹H- and ¹³C-NMR assignments are based on gCOSY, gHMBC, gHSQC, and DEPT-135 experiments. Abbreviations for splitting patterns are as follows: b, broad; s, singlet; d, doublet; t, triplet; m, multiplet etc. Coupling constants are given in Hertz (Hz). High resolution time-of-flight mass spectra were obtained on a Bruker Daltonics micrOTOF mass spectrometer using electrospray ionisation (ESI). Analytical HPLC analyses were carried out on a Waters 2695 Alliance module equipped with a Waters 2996 Photodiode Array Detector (210–350 nm). The chromatographic system consisted of a Hichrom Guard Column for HPLC and a Phenomenex Synergi 4μ MAX-RP 80 A column (150 × 4.60 mm), eluted at 1 mL/min with the following ion-pair buffer: 0.17% (m/v) cetrimide and 45% (v/v) phosphate buffer (pH 6.4) in MeOH. Synthetic phosphates were assayed and quantified by Ames phosphate test^{49 (link)}.

Watt J.M., Graeff R., Thomas M.P, & Potter B.V. (2017). Second messenger analogues highlight unexpected substrate sensitivity of CD38: total synthesis of the hybrid “L-cyclic inosine 5′-diphosphate ribose”. Scientific Reports, 7, 16100.

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Purification and Characterization of Compounds

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Reagents and solvents were purchased from commercial sources and used without further purification, unless described otherwise. Triethylamine was dried with potassium hydroxide, purified by distillation, and stored over potassium hydroxide. MilliQ quality water was used for all aqueous experiments and purifications. All reactions were performed under an inert atmosphere of argon unless otherwise stated. For NMR experiments; ¹H, ¹³C, and ³¹P NMR spectra were collected using either on a Varian Mercury 400 MHz or Bruker Avance III 500 MHz Spectrometer. All ¹H- and ¹³C-NMR assignments are based on COSY, HSQC, HMBC, and DEPT experiments. Chemical shifts (δ) are reported in parts per million (ppm) and splitting patterns are abbreviated as follows: br, broad; s, singlet; d, doublet; t, triplet; m, multiplet etc. High resolution mass spectra (HRMS) were obtained on a Bruker Daltonics micrOTOF mass spectrometer with electrospray ionisation (ESI). Analytical HPLC was performed on a Waters 2695 Alliance module coupled a Waters 2996 PDA Detector (210 – 350 nm) equipped with Hichrom Guard Column for HPLC and a Phenomenex Synergi column (4u, MAX-RP, 80Å, 150 × 4.60 mm), eluted at 1 mL/min with a gradient of MeCN in 0.05 M TEAB. Semi-preparative HPLC was performed on a Waters 2525 pump with manual FlexInject using a Phenomenex Gemini column (5u, C18, 110Å, 250 × 10.00 mm), eluted at 5 mL/min.

Baszczyňski O., Watt J.M., Rozewitz M.D., Fliegert R., Guse A.H, & Potter B.V. (2020). Synthesis of phosphonoacetate analogues of the second messenger adenosine 5′-diphosphate ribose (ADPR). RSC Advances, 10(3), 1776-1785.

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NMR Characterization of 2OX Degradation

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¹H NMR spectra were recorded on either a Varian Mercury 400 MHz or Bruker DRX 500 MHz spectrometer (Bruker, Massachusetts, USA). Diffusion Ordered Spectroscopy (DOSY) experiments were performed using a longitudinal encode-decode (LED) pulse sequence with a 5–95% varying gradient strength over 19 points.
2OX was dissolved in buffers adjusted to a known pH (+/− 0.2 pH units) as measured using either pH paper (Sigma-Aldrich, Missouri, USA) or a pH meter (Mettler Toledo, Ohio, USA). Buffers used were 0.5 M pH 5 sodium acetate, pH 7 sodium phosphate or pH 9 sodium carbonate. Buffers were prepared at the appropriate pH in water, then exchanged 3 × in 99.8% D₂O under vacuum. Reactions were held at constant temperature in a thermostatted oven for periods of up to 6 months.
NMR measurements of 2OX were recorded starting from concentrations of 2, 20 or 200 mM using ~ 0.5 mL volumes in Wilmad NMR tubes (Wilmad Lab Glass, New Jersey, USA) capped under air. Samples were measured periodically, and the kinetics measured by comparison of proton integrations. Results reported in Figure SI4 were conducted at 25° C or 40° C as noted.

Chandru K., Jia T.Z., Mamajanov I., Bapat N, & Cleaves HJ I.I. (2020). Prebiotic oligomerization and self-assembly of structurally diverse xenobiological monomers. Scientific Reports, 10, 17560.

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