Extra rabbit blood was obtained from ongoing studies conducted at the University of California, Irvine, according to NIH Guidelines for the Care and Use of Laboratory Animals, and approved by the Institutional Animal Care and Use Committee 26 . Briefly, New Zealand white rabbits weighing ~ 4 kg were anesthetized and administered 10 mg sodium cyanide dissolved in 60 ml 0.9% NaCl intravenously by pump over 60 min followed by experimental treatments. Serial venous blood samples were obtained at baseline, at time of treatment, and at multiple times thereafter until 90 min following treatment. The blood was immediately cooled to 4° C, centrifuged, and the red blood cells (RBCs) were diluted 10× in ice-cold water resulting in osmotic pressure-driven lysis. Concentration-gradient driven collection of vapor-phase HCN following acidification of the samples with 10% trichloroacetic acid was performed in the same manner as described for both the NBA/DNB and cobinamide-based methods 27 (link).
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Sodium Cyanide
Sodium Cyanide
Sodium Cyanide is a highly toxic chemical compound with the formula NaCN.
It is used in various industrial processes, such as mining, electroplating, and organic synthesis.
Researchers can discover optimized protocols for working with Sodium Cyanide using the AI-driven platform at PubCompare.ai.
This cutting-edge technology helps identify the best protocols and products from literature, pre-prints, and patents to enhance reproducibility and accuracy in Sodium Cyanide research.
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It is used in various industrial processes, such as mining, electroplating, and organic synthesis.
Researchers can discover optimized protocols for working with Sodium Cyanide using the AI-driven platform at PubCompare.ai.
This cutting-edge technology helps identify the best protocols and products from literature, pre-prints, and patents to enhance reproducibility and accuracy in Sodium Cyanide research.
Experieence the future of scientific discovery with PubCompare.ai's innovative solution.
Most cited protocols related to «Sodium Cyanide»
Animals, Laboratory
BLOOD
cobinamide
Cold Temperature
Erythrocytes
Ice
Institutional Animal Care and Use Committees
New Zealand Rabbits
Normal Saline
Osmotic Pressure
Rabbits
Sodium Cyanide
Therapies, Investigational
Trichloroacetic Acid
Veins
Before each individual experiment, cells were loaded during 30 min with 5 μmol/L indo-1/AM or 120 min with 10 μmol/L SBFI, washed twice with fresh Hepes solution (without albumin), and kept for another 15 min to ensure complete de-esterification. Hardware for data recording consisted of a patch clamp amplifier (Axopatch 200B), two home made differential amplifiers for photomultiplier signals and a combined A/D and D/A board (DAS1802AO, Keithley Metrabyte) controlled by custom made software (Test-point).
Loaded myocytes were placed in a thermally controlled (37°C) cell chamber on the stage of an inverted fluorescence microscope (Nikon Diaphot) and superfused with Hepes solution (without albumin) at a rate of 1–2 mL/min. A quiescent rod-shaped myocyte was selected. Action potentials were recorded using the perforated patch clamp technique with a pipette solution containing (mmol/L): [Na+] 6, [K+] 140, [Mg2+] 1.0, [Cl−] 153.6, 1.4, [Hepes] 17, [Glucose] 11, [Ca2+] 2.6, and 0.2 mg/mL amphotericin B (pH 7.1). Pipette resistance was 3–5 MΩ. The potential to bath solution was adjusted to zero. Capacitance and the pipette series resistance were compensated to about 80%. Access resistance to the cell decreased within 10 min after seal formation. Dual wavelength emission fluorescence of Indo-1 was recorded (410/516 nm, excitation at 340 nm) simultaneously with action potential recordings. Free cellular calcium ([Ca2+]i) and total cytoplasmic buffered calcium was calculated as described previously (Baartscheer et al., 1996 (link), 2003b (link)). Fluorescence and action potential signals were digitized at 1 kHz.
In separate experiments, using 2 Hz field stimulation, dual wavelength emission of SBFI was recorded (410/590 nm, excitation at 340 nm) without measurements of action potentials, and [Na+]i was calculated and calibrated as described previously (Baartscheer et al., 1997 (link)).
The increase of [Ca2+]i upon rapid cooling (RC) was used to estimate sarcoplasmic reticulum (SR) calcium content. RC causes complete depletion of calcium from SR and calcium released remains confined to the cytoplasm (Bers, 1987 (link)). RC was performed by rapid superfusion with ice-cold Tyrode's solution of the same composition; low temperature (0–1°C) was reached within 200 ms. Application of RC implies the end of an experiment.
Aerobic metabolism was blocked by 2 mmol/L sodium cyanide and glucose was omitted from the perfusion solution After a control period of 5 min (2 Hz, 37°C).
Loaded myocytes were placed in a thermally controlled (37°C) cell chamber on the stage of an inverted fluorescence microscope (Nikon Diaphot) and superfused with Hepes solution (without albumin) at a rate of 1–2 mL/min. A quiescent rod-shaped myocyte was selected. Action potentials were recorded using the perforated patch clamp technique with a pipette solution containing (mmol/L): [Na+] 6, [K+] 140, [Mg2+] 1.0, [Cl−] 153.6, 1.4, [Hepes] 17, [Glucose] 11, [Ca2+] 2.6, and 0.2 mg/mL amphotericin B (pH 7.1). Pipette resistance was 3–5 MΩ. The potential to bath solution was adjusted to zero. Capacitance and the pipette series resistance were compensated to about 80%. Access resistance to the cell decreased within 10 min after seal formation. Dual wavelength emission fluorescence of Indo-1 was recorded (410/516 nm, excitation at 340 nm) simultaneously with action potential recordings. Free cellular calcium ([Ca2+]i) and total cytoplasmic buffered calcium was calculated as described previously (Baartscheer et al., 1996 (link), 2003b (link)). Fluorescence and action potential signals were digitized at 1 kHz.
In separate experiments, using 2 Hz field stimulation, dual wavelength emission of SBFI was recorded (410/590 nm, excitation at 340 nm) without measurements of action potentials, and [Na+]i was calculated and calibrated as described previously (Baartscheer et al., 1997 (link)).
The increase of [Ca2+]i upon rapid cooling (RC) was used to estimate sarcoplasmic reticulum (SR) calcium content. RC causes complete depletion of calcium from SR and calcium released remains confined to the cytoplasm (Bers, 1987 (link)). RC was performed by rapid superfusion with ice-cold Tyrode's solution of the same composition; low temperature (0–1°C) was reached within 200 ms. Application of RC implies the end of an experiment.
Aerobic metabolism was blocked by 2 mmol/L sodium cyanide and glucose was omitted from the perfusion solution After a control period of 5 min (2 Hz, 37°C).
Action Potentials
Albumins
Amphotericin B
Base Excision Repair
Bath
Calcium
Cells
Cold Temperature
Cytoplasm
Esterification
Exercise, Aerobic
Fluorescence
Glucose
HEPES
indo-1
Metabolism
Microscopy, Fluorescence
Muscle Cells
Perfusion
Phocidae
Sarcoplasmic Reticulum
sodium-binding benzofuran isophthalate
Sodium Cyanide
Tyrode's solution
Acids
antimycin
Antioxidants
benzyloxycarbonylvalyl-alanyl-aspartyl fluoromethyl ketone
Calcium, Dietary
Carbamates
Caspase Inhibitors
Dinoprostone
Epinephrine
Esters
Ethanol
Hypodermic Needles
inhibitors
NADH Dehydrogenase Complex 1
Oligomycins
Pharmaceutical Preparations
physiology
Protein Kinase C-epsilon
Protoplasm
Rotenone
Saline Solution
Sodium Cyanide
Sulfoxide, Dimethyl
Syringes
Thioctic Acid
TMB-8
CPR activity was evaluated according to previously described methods with minor modifications36 (link),37 (link). The microsomal fraction (1 μg microsomal protein) and 400 μM cytochrome c were diluted to 180 μL in 100 mM potassium phosphate buffer (pH 7.4) containing 1.0 mM sodium cyanide. Protein samples (90 μL each) were added to the sample and reference cuvettes. A blank was recorded at 550 nm using a Cary 300 UV–Vis spectrophotometer (Agilent Technologies). Reactions were initiated by the addition of 1.0 mM NADPH diluted in 100 mM potassium phosphate buffer (pH 7.4) containing 1.0 mM sodium cyanide. The control sample contained all reagents except NADPH in a reference cuvette. The absorbance for the microsomal fractions expressing each CYP and CPR was recorded for 2.5 min. The activity of CPR toward cytochrome c was calculated using the extinction coefficient of cytochrome c (21 mM−1 per cm at 550 nm). All experiments were performed in triplicates using a single microsomal preparation.
Buffers
Cytochromes c
Extinction, Psychological
Microsomes
NADP
potassium phosphate
Proteins
Sodium Cyanide
Human cardiac myocytes underwent in vitro chemical I/R as proposed in Ref.24 . Briefly, following 15 minutes aerobic stabilization, the cells were subjected to 9 minutes chemical ischaemia using an inhibitor of cellular respiration and 20 minutes aerobic reperfusion. Cells were subjected to aerobic stabilization and reperfusion in 4‐(2‐hydroxyethyl)‐1‐piperazineethanesulfonic acid (HEPES) buffer (5.5 mmol/L HEPES, 63.7 mmol/L CaCl2, 5 mmol/L KCl, 2.1 mmol/L MgCl2, 5.5 mmol/L glucose, 10 mmol/L taurine) containing additional 55 µmol/L CaCl2 and 0.75 mg/mL BSA. In ischaemia experiments, the cells were subjected to HEPES buffer containing 4.4 mmol/L 2‐deoxyglucose and 4.0 mmol/L sodium cyanide (an inhibitor of electron transport chain). The duration of ischaemia was established in preliminary experiments by measurement of LDH activity released from cells (marker of cell injury). It was determined that 9 minutes of ischaemia was optimal to follow cell recovery during I/R injury (data not shown). At the end of aerobic incubation, the cells were centrifuged for 1 minute at 1500×g at RT and the pellet was suspended in the ischaemia buffer and incubated for 9 minutes at RT. Then the buffer was removed by centrifugation at 1500×g at RT and the pellet was resuspended in the reperfusion HEPES buffer containing additional 55 µmol/L CaCl2 and 0.75 mg/mL mg BSA and incubated for 20 minutes at RT temperature. After reperfusion, the myocytes were centrifuged at 1500×g for 5 minutes at RT and the pellet was homogenized and the resultant homogenate stored until assayed at −80°C. In aerobic control experiments, the myocytes were aerobically maintained for the duration of the experiment. In I/R experiments examining the effect of barbiturate, the cells were subjected to I/R in the presence of increasing concentrations of the tested compound (0.1, 1.0 and 10 μmol/L) for 10 minutes before ischaemia and for first the 10 minutes of I/R.
2-Deoxyglucose
Acids
barbiturate
Buffers
Cell Respiration
Cells
Centrifugation
Electron Transport
Exercise, Aerobic
Glucose
HEPES
Homo sapiens
Injuries
Ischemia
Magnesium Chloride
Muscle Cells
Myocytes, Cardiac
Reperfusion
Sodium Cyanide
Taurine
Most recents protocols related to «Sodium Cyanide»
FeIIITPPS (F), Py3CD (P), and Im3CD (I) were synthesized in our laboratory. The synthetic procedures were previously reported (46 (link), 48 , 70 (link)). Sodium dithionite (S), sodium cyanide (NaCN), phosphate-buffered saline (PBS), and other chemicals were purchased from Fujifilm Wako.
Phosphates
Saline Solution
Sodium Cyanide
Sodium Dithionite
The synthesis of bis-benzoxazolyl phenol derivatives is shown in Scheme S2 . A mixture of 2-hydroxyisophthalaldehyde derivatives (3.0 mmol), 2-aminophenol (0.655 g, 6.0 mmol), and phenylboronic acid (0.109 g, 0.9 mmol) in 30 mL of MeOH was magnetically stirred for 5 min. Sodium cyanide (0.192 g, 4.8 mmol) was added. The mixture was thereafter stirred for 18 h at 25 °C. The flask was subsequently immersed in an ice bath. The precipitate was collected via vacuum filtration and washed with cold water. The solid was purified by recrystallization from MeOH/H2O.
The compound 2,6-bis(2-benzoxazolyl)-4-methylphenol (C1 ) was obtained as an orange solid (0.569 g, 55.4%). m.p: 172.1–175.6 °C; 1H-NMR (400 MHz, DMSO-d6) δ 12.20 (s, 1H), 8.09 (s, 2H), 7.84–7.80 (m, 4H), 7.48–7.41 (m, 4H), 2.40 (s, 3H); 13C-NMR (101 MHz, DMSO-d6) δ 161.8, 155.3, 149.9, 140.6, 133.5, 129.7, 126.5, 125.7, 120.1, 113.7, 111.6, 20.3; HRMS (ESI): m/z calcd for C21H13N2O3 [M–H]− 341.0931, found 341.0923.
The compound 2,6-bis(2-benzoxazolyl)-4-methylphenol (
1H NMR
2-aminophenol
Anabolism
Bath
benzeneboronic acid
Carbon-13 Magnetic Resonance Spectroscopy
Cold Temperature
derivatives
Filtration
para-cresol
Phenol
Sodium Cyanide
Sulfoxide, Dimethyl
Vacuum
PANC-1 human pancreatic cancer cells were maintained in high-glucose DMEM supplemented with 10% fetal bovine serum and 1% penicillin/streptomycin. Cells were pelleted, re-suspended in culture medium supplemented with 2% agarose and loaded into fluorinated ethylene-propylene (FEP) tubing suspended in a water bath (Fig. 1 ). Cells were exposed to 1 mM sodium cyanide to induce known metabolic perturbations, with images taken every 3 minutes.
Bath
Cells
Culture Media
Fetal Bovine Serum
fluorinated ethylene propylene
Glucose
Homo sapiens
Pancreatic Cancer
Penicillins
Sepharose
Sodium Cyanide
Streptomycin
Lipidoids were synthesized as previously described (97 (link)). Specifically, the amines 306 and 200 were reacted with the tail isodecyl acrylate (Oi10) at a molar ratio of 1:4 to form the lipidoids 306Oi10 and 200Oi10, respectively. The amine 514 was synthesized by reacting 2-hexyl-decyl acrylate with sodium cyanide to form a nitrile, which was subsequently reduced to a primary amine with lithium aluminum hydride (97 (link)). Branched tail O6,10 was synthesized by reacting alcohol (2-hexyl-decanol, Sigma-Aldrich) with acryloyl chloride (Alfa Aesar) and trimethylamine (Sigma-Aldrich) in a molar ratio of 1:1.5:2 in reagent grade acetone (Spectrum) in a round bottom flask on ice. Ice was removed after 10 min, and the flask was equilibrated to room temperature for 2 hours. The reaction was quenched with 3 ml of deionized water for 10 min. Product was then rotary evaporated for approximately 1.5 hours, dissolved in ethyl acetate, and placed in a separation funnel. Four washes were done to remove contaminants: (i) NaCl (saturated) and water in 1:1 molar ratio, (ii) 1 M HCl and water in 1:1 molar ratio, (iii) NaHCO3 (saturated), and (iv) NaCl (saturated). Product was then retrieved, and 3 to 6 mg of 2,5-di-tert-butylhydroquinone (Sigma-Aldrich) was added to prevent polymerization. Magnesium sulfate (Fisher Chemicals) was then added to remove water and then filtered out. Product was rotary evaporated to remove solvent. Tail purification was done using Teledyne ISCO Chromatography with a gradual increase to 40% of dichloromethane:methanol:ammonium hydroxide (60:30:10) in dichloromethane as the model phase and silica as the solid. Structure was confirmed with H-1 and C-13 nuclear magnetic resonance (500 Hz). Amines and tails were combined in glass scintillation vials and stirred at 90°C for 3 days without solvent. The lipidoids were purified using a Teledyne ISCO Chromatography system (Thousand Oaks, CA) to isolate the fully substituted lipidoid product. The structures of the final products are shown in fig. S1.
2,5-di-tert-butylhydroquinone
Acetone
acrylate
acryloyl chloride
Amines
Ammonium Hydroxide
Bicarbonate, Sodium
Chromatography
Ethanol
ethyl acetate
hexyl acrylate
lithium aluminum hydride
Magnetic Resonance Imaging
Methanol
Methylene Chloride
Molar
Nitriles
Polymerization
Quercus
Silicon Dioxide
Sodium Chloride
Sodium Cyanide
Solvents
Sulfate, Magnesium
Tail
trimethylamine
5,5′,6,6′-tetrachloro-1,1′,3,3′-tetraethylbenzimidazolylcarbocyanine iodide (JC-1) was purchased from Molecular Probes (Eugene, Oregon, USA). Carbonyl cyanide-4-(trifluoromethoxy)phenylhydrazone (FCCP), colchicine, latrunculin A, nisoldipine, (S)-(−)-Bay K8644 (BayK(−)) and sodium cyanide (NaCN) were bought from Merck (Kenilworth, New Jersey, USA). Jasplakinolide was purchased from Cayman Chemical (Ann Arbor, Michigan, USA); (R)-(+)-Bay K8644 (BayK(+)) from BioVision (Milpitas, California, USA); and CD-29 from BD Biosciences (Franklin Lakes, New Jersey, USA). AID-TAT peptide was synthesized using the amino acid sequence QQLEEDLKGYLDWITQAE including a cell-penetrating TAT sequence (RKKRRQRRR) tethered via 6-aminohexanoic acid (AusPep, Tullamarine, Victoria, AUS)50 (link). The AHNAK-P4N-TAT peptide was synthesized using the amino acid sequence KGKHGKLKFGTFGGLGSKSKGHYEVT tethered to the TAT sequence as previously described (Mimotopes Pty Ltd, Victoria, AUS).
Mitochondrial membrane potential (Ψm) was assessed using fluorescent indicator JC-1 (200 nM, incubation period = 3 h, ex = 480 nm, em = 580/535 nm, interval = 2 min, exposure = 50 ms)16 (link),17 (link). At the end of each experiment, mitochondrial electron transport blocker sodium cyanide was applied to collapse Ψm, confirming that the JC-1 signal was indicative of Ψm (NaCN, 40 mM). Mitochondrial flavoprotein oxidation was assessed by recording myocyte autofluorescence as previously described (ex = 480 nm, em = 535 nm, interval = 1 min, exposure = 250 ms)16 (link),17 (link). Mitochondrial electron transport chain uncoupler FCCP (50 μM) was added at the end of each experiment to increase flavoprotein oxidation, confirming signal was mitochondrial in origin. All in vitro fluorescence was measured on an Andor Zyla SCMOS 5.5 MP camera attached to an inverted Nikon TE2000-U microscope. Ratiometric JC-1 or flavoprotein fluorescent images were quantified using Metamorph 7.10. Regions containing myocytes were manually traced to obtain a fluorescent signal for each cell. An equivalent region not containing cells was used as background and subtracted for each cell. Responses to treatments were reported as a percentage increase or decrease from the pre-treatment (basal) average.
Mitochondrial membrane potential (Ψm) was assessed using fluorescent indicator JC-1 (200 nM, incubation period = 3 h, ex = 480 nm, em = 580/535 nm, interval = 2 min, exposure = 50 ms)16 (link),17 (link). At the end of each experiment, mitochondrial electron transport blocker sodium cyanide was applied to collapse Ψm, confirming that the JC-1 signal was indicative of Ψm (NaCN, 40 mM). Mitochondrial flavoprotein oxidation was assessed by recording myocyte autofluorescence as previously described (ex = 480 nm, em = 535 nm, interval = 1 min, exposure = 250 ms)16 (link),17 (link). Mitochondrial electron transport chain uncoupler FCCP (50 μM) was added at the end of each experiment to increase flavoprotein oxidation, confirming signal was mitochondrial in origin. All in vitro fluorescence was measured on an Andor Zyla SCMOS 5.5 MP camera attached to an inverted Nikon TE2000-U microscope. Ratiometric JC-1 or flavoprotein fluorescent images were quantified using Metamorph 7.10. Regions containing myocytes were manually traced to obtain a fluorescent signal for each cell. An equivalent region not containing cells was used as background and subtracted for each cell. Responses to treatments were reported as a percentage increase or decrease from the pre-treatment (basal) average.
Acids
Amino Acid Sequence
Bay-K-8644
Caimans
Carbonyl Cyanide p-Trifluoromethoxyphenylhydrazone
Cells
Colchicine
Electron Transport
Flavoproteins
Fluorescence
Genes, Mitochondrial
Iodides
jasplakinolide
latrunculin A
Membrane Potential, Mitochondrial
mesoxalonitrile
Microscopy
Mitochondrial Inheritance
Molecular Probes
Muscle Cells
Nisoldipine
Peptides
phenylhydrazone
Shock
Signal Transduction
Sodium Cyanide
tat peptide (49-57), Human immunodeficiency virus 1
Top products related to «Sodium Cyanide»
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Sodium cyanide is a chemical compound with the formula NaCN. It is a white, crystalline solid that is commonly used in various industrial applications. The core function of sodium cyanide is as a reagent in metallurgical processes, particularly in the extraction of gold and silver from ores.
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Potassium chloride (KCl) is an inorganic compound that is commonly used as a laboratory reagent. It is a colorless, crystalline solid with a high melting point. KCl is a popular electrolyte and is used in various laboratory applications.
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DMSO is a versatile organic solvent commonly used in laboratory settings. It has a high boiling point, low viscosity, and the ability to dissolve a wide range of polar and non-polar compounds. DMSO's core function is as a solvent, allowing for the effective dissolution and handling of various chemical substances during research and experimentation.
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The ELISA plate reader is a laboratory instrument designed to measure the absorbance of samples in a microplate format. It is commonly used to quantify the presence of specific proteins, antibodies, or other analytes in biological samples through enzyme-linked immunosorbent assay (ELISA) techniques.
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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.
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NaCl is a chemical compound commonly known as sodium chloride. It is a white, crystalline solid that is widely used in various industries, including pharmaceutical and laboratory settings. NaCl's core function is to serve as a basic, inorganic salt that can be used for a variety of applications in the lab environment.
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Sodium hydroxide is a chemical compound with the formula NaOH. It is a white, highly caustic crystalline solid that is commonly used as a strong base in various industrial and laboratory applications.
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Sodium succinate is a chemical compound used as a lab equipment product. It serves as a source of the succinate ion, which is an important intermediate in the citric acid cycle, a fundamental metabolic pathway in living organisms.
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Potassium thiocyanate is a chemical compound with the formula KSCN. It is a colorless, crystalline solid that is widely used in various laboratory applications. The core function of potassium thiocyanate is as a reagent in analytical chemistry, particularly in the detection and quantification of certain metal ions.
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Sodium cyanide (NaCN) is an inorganic compound that consists of a sodium cation (Na+) and a cyanide anion (CN−). It is a white, crystalline solid that is highly soluble in water. Sodium cyanide is commonly used as a precursor in the production of other chemicals and in various industrial processes.