Log In Sign up
The largest database of trusted experimental protocols
> Chemicals & Drugs > Inorganic Chemical > Hydrazine

Hydrazine

Hydrazine is a colourless, flammable, and toxic chemical compound with the formula N2H4.
It is widely used as a propellant in spacecraft rocket engines and as a reducing agent in various industrial processes.
Hydrazine research explores its applications, synthesis, properties, and potential health and environmental impacts.
PubCompare.ai's platform enables researchers to efficiently locate and compare the best hydrazine research protocols from literature, preprints, and patents, optimizing reproducibility and accuracy.
This cutting-edge tool streamlines hydrazine research by leveraging intelligent comparisons to support scientific discovery and innovation.

Most cited protocols related to «Hydrazine»

1
Metabolic Network Analysis with MetaboNetworks
First, the appropriate data from KEGG has to be imported to Matlab. In MetaboNetworks this is done using a function that uses the KEGG REST-API to calculate a metabolite adjacency matrix that can later be used to draw the graphs. The user can select one or multiple organisms for which complete genomes are available in KEGG; for these organisms a list of enzymes (with E.C. numbers) that are associated with a gene from any of the organisms is determined. Using this enzyme list, all reactions are queried and enzymes involved in the reactions are matched against the enzyme list. Only reactions that require an enzyme from the list or that are listed as ‘non-enzymatic’ or ‘spontaneous’ are used to find their main reaction pairs. The compounds from these reaction pairs are considered adjacent. Each row/column in the adjacency matrix indicates a specific compound (with a KEGG compound ID) and a list of all names for these compounds are found from the KEGG compound database. A reaction database has previously been collected using a similar approach (Ma and Zeng, 2003 (link)) to MetaboNetworks, however, that database includes reactions from all species, whereas MetaboNetworks focusses on organisms of interest as not all reactions can occur in all organisms.
Second, when the data collection is complete, MetaboNetworks can be used to create and explore custom networks. A list of metabolites, e.g. biomarkers arising from a metabonomic experiment, can be passed to MetaboNetworks and it searches for the shortest path between each of these metabolites using the breadth-first search algorithm. All compounds that are a part of a shortest path between any of the metabolites are included in the network. By default, MetaboNetworks plots the network as a circular graph. Other graph layouts include a spring-embedded layout, high-dimensional embedding and two types of uniform edge-length layouts, the last aim to place nodes with as little overlap as possible. If the Matlab statistical toolbox is installed, multidimensional scaling can also be used.
Last, when the initial network layout is satisfactory the graph layout can be manually adjusted. Supported adjustments include node position, node/edge removal, highlighting nodes (see green edges of nodes in Fig. 1), and shortest paths (orange edges in Fig. 1), node text and nodes/edge/text properties (font, width, size, etc.). If additional data is supplied, the association of the metabolites with a response variable can be shown as node colour (see Fig. 1). Furthermore, the network can be exported as a tif, png, pdf, eps or other image formats, the network can always be reset to the original graph (all changes are lost). Another option is to click on a node to open a web browser showing the compound entry in KEGG or show reactions pairs in KEGG of selected nodes. The Supplementary Information includes a full walkthrough of the software and all the capabilities.

Shows the graphical user-interface of MetaboNetworks with a custom network drawn for significant metabolites from a hydrazine toxicity study in rats (Nicholls et al., 2001 (link)). Metabolites higher in hydrazine-dosed rats compared with controls are shown in red, and metabolites lower in hydrazine-dosed rats are shown in blue. The white nodes are part of shortest paths between the coloured nodes. The edges shown in orange are part of the shortest path (four reactions) between taurine and glycine. Aside from the rat, all bacteroidetes and firmicutes species were included in the database

Posma J.M., Robinette S.L., Holmes E, & Nicholson J.K. (2013). MetaboNetworks, an interactive Matlab-based toolbox for creating, customizing and exploring sub-networks from KEGG. Bioinformatics, 30(6), 893-895.
Full text: Click here
Publication 2013
Bacteroidetes Biological Markers Enzymes Firmicutes Genes Genome Glycine hydrazine Taurine
2
Synthesis and Characterization of Hydrazine-Derived Compounds
Chemical synthesis of potential inhibitors. Reagents and solvents were from Aldrich, Alfa Aesar or Acros. Reactions were monitored by TLC, which was performed on precoated aluminum-backed plates (Merck, silica 60 F254). Melting points were determined using a Leica Galen III hot-stage melting point apparatus and microscope. Infrared spectra were recorded from Nujol mulls between sodium chloride discs, on a Bruker Tensor 27 FT-IR spectrometer. NMR spectra were acquired using a Bruker DPX500 NMR spectrometer. Chemical shifts (δ) are given in ppm, and the multiplicities are given as singlet (s), doublet (d), triplet (t), quartet (q), multiplet (m), broad (br). Coupling constants J are given in Hz (± 0.5 Hz). High resolution mass spectra (HRMS) were recorded using a Bruker MicroTOF spectrometer. The purity of all compounds synthesized were ≥95% as determined by analytical reverse-phase HPLC (Ultimate 3000). Daminozide (Alar™) and compound 28 are commercially available. The synthesis and characterisation of compounds 2225 , 2526 (link), 2727 , 3628 , 3729 and 3826 (link) has been reported. The synthesis of compounds 31-35, 39-41 and 13C NMR spectra for 22, 23, 24, 26, 31-35 are given in the Supporting Information.
4-(2,2,2-Trimethylhydrazinyl)-4-oxobutanoate 22. The synthesis of compound 22 was as reported25 , thus reaction of daminozide (500mg, 3.1 mmol) with methyl iodide (700mg, 0.31 mL, 5.0 mmol) gave 22 as a white solid (75% yield), mp: 137-138 °C (lit.1 137-138.5 °C); 1H NMR (500 MHz, MeOD): δ 2.40 (t, J = 6.5 Hz, 2H), 2.51 (t, J = 6.5 Hz, 2H), 3.56 (s, 9H); 13C NMR (125 MHz, MeOD): δ 28.5, 29.1, 56.1, 170.4, 173.4; IR (neat) υ/cm−1: 3405, 3312, 1729, 1693; HRMS (m/z): [M]+ calcd. for C7H15N2O3, 175.1077; found, 175.1081.
General procedure for the coupling of hydrazine to succinic anhydride. To a stirred solution of the appropriate hydrazine (1 equiv.) in acetonitrile (5 mL) was added dropwise a solution of succinic anhydride (200 mg, 2.0 mmol, 1 equiv.) in acetonitrile (5 mL). The mixture was stirred at room temperature for 24 h, after which the solvent was evaporated in vacuo and the resulting crude purified using semipreparative reverse-phase HPLC, performed on a phenomenex C18 column (150 mm × 4.6 mm). Separation was achieved using a linear gradient of solvent A (water + 0.1% CF3CO2H) and solvent B (acetonitrile + 0.1% CF3CO2H), eluting at a flow rate of 1 mL/min and monitoring at 220 nm: 0% B to 40% B over 30 min.
4-(2-Methylhydrazinyl)-4-oxobutanoic acid 23. Compound 23 is a colourless oil (63% yield), 1H NMR (500 MHz, DMSO-d6): δ 2.35 (t, J = 7.0 Hz, 2H), 2.68 (t, J = 7.0 Hz, 2H), 2.98 (s, 3H), 4.76 (s, 1H), 7.74 (s, 1H); 13C NMR (125 MHz, DMSO-d6): δ 28.3, 29.1, 170.1, 173.6; IR (neat) υ/cm−1: 33 3219, 3057, 1708, 1632; HRMS (m/z): [M+Na]+ calcd. for C5H10N2NaO3, 169.0584; found, 169.0577.
4-Hydrazinyl-4-oxobutanoic acid 24. Compound 24 is a colourless oil (87% yield), 1H NMR (500 MHz, DMSO-d6): δ 2.34 (t, J = 7.0 Hz, 2H), 2.60 (t, J = 7.0 Hz, 2H), 5.86 (s, 1H), 8.99 (s, 1H); 13C NMR (125 MHz, DMSO-d6): δ 28.2, 29.1, 170.8, 173.9; IR (neat) υ/cm−1: 3303, 3290, 3199, 1712, 1624; HRMS (m/z): [M-H]- calcd. for C4H7N2O3, 131.0462; found, 131.0468.
4-Oxo-4-(1,2,2-trimethylhydrazinyl)butanoic acid 26. Compound 26 is a white solid (56% yield), mp: 97-98 °C, 1H NMR (500 MHz, DMSO-d6): δ 2.37 (t, J = 7.0 Hz, 2H), 2.66 (t, J = 7.0 Hz, 2H), 2.74 (s, 3H), 11.98 (s, 1H); 13C NMR (125 MHz, DMSO-d6): δ 28.2, 29.8, 43.4, 48.7, 173.5, 175.0; IR (neat) υ/cm−1: 2958, 1723, 1615; HRMS (m/z): [M+Na]+ calcd. for C7H14N2NaO3, 197.0897; found, 197.0895.
4-((Dimethylamino)oxy)-4-oxobutanoic acid 29. N,N-Dimethylhydroxylamine (39 mg, 0.63 mmol, 1.1 equiv. ) was added to a solution of 4-(tert-butoxy)-4-oxobutanoic acid (100 mg, 0.57 mmol, 1 equiv.), hydroxybenzotriazole (100 mg, 0.74 mmol, 1.3 equiv.), 1-ethyl-3-(3-dimethylaminopropyl) carbodiimide ( 140 mg, 0.74 mmol, 1.3 equiv.) and diisopropylethylamine ( 0.2 mL, 1.14 mmol, 2.0 equiv.) in CH2Cl2 (10 mL). The reaction was stirred at room temperature overnight, washed with water, HCl 1N, brine, dried on MgSO4. The organic phase was evaporated in vacuo and purified by chromatography (MeOH/CH2Cl2 0.5/9.5) to obtain 110 mg of tert-butyl 4((dimethylamino)oxy)-4-oxobutanoate (90% yield). CF3CO2H (0.04 ml, 0.37 mmol, 4 equiv.) was added to a solution of tert-butyl 4((dimethylamino)oxy)-4-oxobutanoate (20 mg, 0.09 mmol, 1 equiv.) in CH2Cl2 (1.5 ml). The reaction was stirred at room temperature for 4h and evaporated in vacuo to give 14 mg of 29 (yield 95%). 1H NMR (500 MHz, CD3OD) δ 2.59 (s, 6H), 2.57 (s, 4H); 13C NMR (500 MHz, CD3OD) δ 176.2, 172.0, 48.5, 29.9; IR (neat) 3341, 2485,1717, 1120, 1026, 975 cm−1; HRMS (m/z):[M+]calcd. for C6H11NO4 161.0688; found 161.0923.
N‘1, N‘1, N‘4, N‘4-Tetramethylsuccinohydrazide 30. A solution of succinic acid (100 mg, 0.85 mmol, 1 equiv.), hydroxybenzotriazole (350 mg, 2.11 mmol, 2.3 equiv.), 1-ethyl-3-(3-dimethylaminopropyl)carbodiimide (421 mg, 2.11 mmol, 2.3 equiv.), diisopropylethylamine (0.6 mL, 3.4 mmol, 4 equiv.) and 1,1-dimethylhydrazine (0.16 mL, 2.04 mmol, 2.2 equiv.) in CH2Cl2 (20 mL) was stirred at room temperature overnight. CH2Cl2 (10 mL) was added and the reaction mixture was washed with water, a saturated solution of NaHCO3, brine and dried on MgSO4. The organic phase was evaporated in vacuo and purified by chromatography (MeOH/ CH2Cl2 1/9) to give 77 mg of 30 (45% yield). 1H NMR (500 MHz, CD3OD) δ 2.87 (s, 6H), 2.65 (s, 2H); 13C NMR (500 MHz, CD3OD) δ 178.2, 43.8, 27.6; IR (neat) 3356, 2485, 2071, 1695, 1120, 1027, 974 cm−1; HRMS (m/z):[(M-2CH3)−]calcd. for C6H14N4O2, 174.1117; found, 174.1022.
Rose N.R., Woon E.C., Tumber A., Walport L.J., Chowdhury R., Li X.S., King O.N., Lejeune C., Ng S.S., Krojer T., Chan M.C., Rydzik A.M., Hopkinson R.J., Che K.H., Daniel M., Strain-Damerell C., Gileadi C., Kochan G., Leung I.K., Dunford J., Yeoh K.K., Ratcliffe P.J., Burgess-Brown N., von Delft F., Muller S., Marsden B., Brennan P.E., McDonough M.A., Oppermann U., Klose R.J., Schofield C.J, & Kawamura A. (2012). The Plant Growth Regulator Daminozide is a Selective Inhibitor of the Human KDM2/7 Histone Demethylases. Journal of medicinal chemistry, 55(14), 6639-6643.
Publication 2012
3
Comprehensive Oxidative Stress Assessment
Assessment of superoxide anion (O2.-) generation. Superoxide anion generation was determined by a standard assay.48 (link) Briefly, 0.1 µg/ml of PMA (Sigma), a potent macrophage stimulant, and 0.12 mM horse heart cytochrome-c (Sigma) were added to isolated cell suspensions after treatment schedule, and washing with PBS. Cytochrome-c reduction by generated superoxide was then determined by spectrophotometric absorbance at a 550 nm wavelength. Results are expressed n mol of cytochrome-c reduced/min, using extinction-coefficient 2.1 × 104 M−1 cm−1.
NADPH oxidase activity. After the treatment schedule, the macrophages of different groups prewarmed in Krebs ringer buffer (KRB) with 10 mM glucose at 37°C for 3 min. PMA (0.1 µg/ml) prewarmed at 37°C for 5 min was added, and the reaction was stopped by putting in ice. Centrifugation was carried out at 400 g for 5 min and the resultant pellet was resuspended in 0.34 M sucrose. The cells were then lysed with hypotonic lysis buffer. Centrifugation was carried out at 800 xg for 10 min and the supernatant used to determine enzyme activity. NADPH oxidase activity was determined spectrophotometrically by measuring cytochrome c reduction at 550 nm. The reaction mixture contained 10 mM phosphate buffer (pH 7.2), 100 mM NaCl, 1 mM MgCl2, 80 µM cytochrome c, 2 mM NaN3 and 100 µl of supernatant (final volume 1.0 ml). A suitable amount of NADPH (10–20 µl) was added last to initiate the reaction.49 (link)
Myeloperoxidase (MPO) activity. 200 µl of cell lysate was reacted with 200 µl substrate (containing H2O2 and OPD) in dark for 30 min. The blank was prepared with citrate phosphate buffer (pH 5.2) and substrate, in absence of cell free supernatant. The reaction was stopped with addition of 100 µl 2(N) sulfuric acid and reading was taken at 492 nm in a spectrophotometer.50
Determination of lipid peroxidation (MDA). Lipid peroxidation was estimated by the method of Ohkawa et al. in cell lysate.51 (link) Briefly, the reaction mixture contained Tris-HCl buffer (50 mM, pH 7.4), tert-butyl hydroperoxide (BHP) (500 µM in ethanol) and 1 mM FeSO4. After incubating the samples at 37°C for 90 min, the reaction was stopped by adding 0.2 ml of 8% sodium dodecyl sulfate (SDS) followed by 1.5 ml of 20% acetic acid (pH 3.5). The amount of malondialdehyde (MDA) formed during incubation was estimated by adding 1.5 ml of 0.8% TBA and further heating the mixture at 95°C for 45 min. After cooling, samples were centrifuged, and the TBA reactive substances (TBARS) were measured in supernatants at 532 nm by using 1.53 × 105 M−1 cm−1 as extinction coefficient. The levels of lipid peroxidation were expressed in terms of n mol/mg protein.
Protein carbonyls contents (PC). Protein oxidation was monitored by measuring protein carbonyl contents by derivatization with 2, 4-dinitrophenyl hydrazine (DNPH).52 (link) In general, cell lysate proteins in 50 mM potassium phosphate buffer, pH 7.4, were derivatized with DNPH (21% in 2 N HCl). Blank samples were mixed with 2 N HCl incubated at 1 h in the dark; protein was precipitated with 20% trichloro acetic acid (TCA). Underivatized proteins were washed with an ethanol:ethyl acetate mixture (1:1). Final pellets of protein were dissolved in 6.0 N guanidine hydrochloride and absorbance was measured at 370 nm. Protein carbonyls content was expressed in terms of µ mol/mg protein.
Activity of super oxide dismutase (SOD). SOD activity was determined from its ability to inhibit the auto-oxidation of pyrogalol according to Mestro Del and McDonald.53 The reaction mixture considered of 50 mM Tris (hydroxymethyl) amino methane (pH 8.2), 1 mM diethylenetriamine penta acetic acid, and 20–50 µl of cell lysate. The reaction was initiated by addition of 0.2 mM pyrogalol, and the absorbance measured kinetically at 420 nm at 25°C for 3 min. SOD activity was expressed as unit/mg protein.
Activity of catalase (CAT). Catalase activity was measured in the cell lysate by the method of Luck.54 The final reaction volume of 3 ml contained 0.05 M Tris-buffer, 5 mM EDTA (pH 7.0), and 10 mM H2O2 (in 0.1 M potassium phosphate buffer, pH 7.0). About 50 µl aliquot of the cell lysates were added to the above mixture. The rate of change of absorbance per min at 240 nm was recorded. Catalase activity was calculated by using the molar extinction coefficient of 43.6 M−1 cm−1 for H2O2. The level of CAT was expressed in terms of m mol H2O2 consumed/min/mg protein.
Determination of reduced glutathione (GSH). Reduced glutathione estimation in the cell lysate was performed by the method of Moron et al.55 (link) The required amount of the cell lysate was mixed with 25% of trichloroacetic acid and centrifuged at 2,000 xg for 15 min to settle the precipitated proteins. The supernatant was aspirated and diluted to 1 ml with 0.2 M sodium phosphate buffer (pH 8.0). Later, 2 ml of 0.6 mM DTNB was added. After 10 minutes the optical density of the yellow-colored complex formed by the reaction of GSH and DTNB (Ellman's reagent) was measured at 405 nm. A standard curve was obtained with standard reduced glutathione. The levels of GSH were expressed as µg of GSH/mg protein.
Oxidized glutathione level (GSSG). The oxidized glutathione level was measured after derevatization of GSH with 2-vinylpyidine according to the method of Griffith.56 (link) In brief, with 0.5 ml cell lysate, 2 µl 2-vinylpyidine was added and incubates for 1 hr at 37°C. Then the mixture was deprotenized with 4% sulfosalicylic acid and centrifuged at 1,000 xg for 10 min to settle the precipitated proteins. The supernatant was aspirated and GSSG level was estimated with the reaction of DTNB at 412 nm in spectrophotometer and calculated with standard GSSG curve.
Redox ratio (GSH/GSSG). Redox ratio was determined for all the seven groups by taking the ratio of reduced glutathione/oxidized glutathione.
Activity of glutathione peroxidase (GPx). The GPx activity was measured by the method of Paglia and Valentine.57 (link) The reaction mixture contained 50 mM potassium phosphate buffer (pH 7.0), 1 mM EDTA, 1 mM sodium azide, 0.2 mM NADPH, 1 U glutathione reductase and 1 mM reduced glutathione. The sample, after its addition, was allowed to equilibrate for 5 min at 25°C. The reaction was initiated by adding 0.1 ml of 2.5 mM H2O2. Absorbance at 340 nm was recorded for 5 min. Values were expressed as n mol of NADPH oxidized to NADP by using the extinction coefficient of 6.2 × 103 M−1 cm−1 at 340 nm. The activity of GPx was expressed in terms of n mol NADPH consumed/min/mg protein.
Activity of glutathione reductase (GR). The GR activity was measured by the method of Miwa.58 The tubes for enzyme assay were incubated at 37°C and contained 2.0 ml of 9 mM GSSG, 0.02 ml of 12 mM NADPH, Na4, 2.68 ml of 1/15 M phosphate buffer (pH 6.6) and 0.1 ml of cell lysate. The activity of this enzyme was determined by monitoring the decrease in absorbance at 340 nm. The activity of GR was expressed in terms of n mol NADPH consumed/min/mg protein.
Activity of glutathione-s-transferase (GST). The activity of GST activity was measured by the method of Habig et al.59 (link) The tubes of enzyme assay were incubated at 25°C and contained 2.85 ml of 0.1 M potassium phosphate (pH 6.5) containing 1 mM of GSH, 0.05 ml of 60 mM 1-chloro-2, 4-dinitrobengene and 0.1 ml cell lysate. The activity of this enzyme was determined by monitoring the increase in absorbance at 340 nm.
Protein estimation. Protein was determined according to Lowry et al. using bovine serum albumin as standard.60
Mahapatra S.K., Chakraborty S.P., Das S, & Roy S. (2009). Methanol extract of Ocimum gratissimum protects murine peritoneal macrophages from nicotine toxicity by decreasing free radical generation, lipid and protein damage and enhances antioxidant protection. Oxidative Medicine and Cellular Longevity, 2(4), 222-230.
Publication 2009
4
Curation and Analysis of Diverse Molecular Databases
Here, the MDDR and ACD databases were chosen as representatives for drug-like and non-drug-like datasets, respectively. The Traditional Chinese Medicine Compound Database (TCMCD) was developed in our group [23 (link),28 ]. The latest version of TCMCD has 63,759 organic molecules identified from more than 5,000 herbs in TCMs. All the molecules in these three databases were minimized in MOE [29 ] by using molecular mechanics (MM) with the MMFF94 force field [30 (link)]. The three databases were preprocessed using the following protocol [6 (link),31 (link),32 (link)]: (1). Molecules were examined for bad valence states, and molecules containing one or more atoms with bad valence states were removed; (2). The salt fragments in the input molecules were identified and removed; (3). The molecules with atoms other than C, H, O, N, P, S, F, Cl, Br and I were removed; (4). The solvent molecules in the input molecules were identified and removed; (5). The input molecules with multiple organic parts were identified and the largest connected structural fragment in each input molecule was reserved; (6). Duplicates were removed in each individual database; (7). Identical compounds found in both ACD and MDDR databases were removed from ACD. For MDDR, antineoplastic drugs were removed because they are often highly cytotoxic and are likely to react with protein targets. In addition, the compounds (adsorption promoters, anesthetics, diagnostic agents (isotope), diagnostics for AIDS, diagnostics for cancer, drug delivery systems, magnetic resonance imaging agents, sweeteners, and dental agents) without therapeutic activity were eliminated from MDDR. As a result, we got 2,175,382 molecules from ACD, 142,747 molecules from MDDR and 63,759 molecules from TCMCD for the following analysis.
It should be noted that we did not remove compounds with reactive functional groups. We did a survey on how many reactive compounds in three data sets. A simple filter was designed to remove compounds with reactive functional groups, and the reactive functional groups used by us include aldehyde, alkyl-halide, anhydride, diazo, dicarbonyl, disulfide, hydrazine-N-NH2, isocyanate, isothiocyanates, peroxide, quaternaryamine and acyl-halide.[6 (link)] When this filter was applied, ~5% of compounds in MDDR were removed as reactive molecules; however, ~6% of launched drugs in MDDR were also removed as reactive molecules. Moreover, based on Opera’s analysis, removing reactive compounds from ACD and MDDR does not have obvious impact on the performance of the drug-likeness filters [3 (link)], so we did not remove the molecules with reactive functional groups.
It is well-known that too large molecules usually do not have good absorption property [33 ,34 (link)], and therefore we set the cutoff for molecular weight (MW) to be 600, and the sub-databases, namely ACD1, MDDR1 and TCMCD1, respectively, were constructed by only choosing the molecules with MW less than 600. Furthermore, to examine the influence of the MW cutoff on our analysis, three more subsets (ACD2, MDDR2 and TCMCD2) with MW less than 800 were generated. The numbers of the compounds in MDDR1, ACD1 and TCMCD1 are 123,927, 1,999,530 and 50,962, respectively, and the numbers of the compounds in MDDR2, ACD2 and TCMCD2 are 138,507, 2,007,594 and 57,809, respectively.
Comparison study showed that the mean MW of compounds in ACD1 was about 120 less than that of compounds in MDDR1. It is believed that many molecular properties are dependent on MW, and so in order to construct the filters or models of drug-likeness unrelated to MW, a subset of ACD1 designated as ACD3 and a subset of TCMCD1 labeled as TCMCD3 were constructed, and ACD3, TCMCD3 and MDDR1 have almost the same MW distributions. In total, there are 123,927 123,929 and 33,961 entries in ACD3, MDDR1 and TCMCD3, respectively. For the purpose of performing principal component analysis (PCA), the same number of entries as that of TCMCD3 (33,961) were randomly selected from MDDR1 and ACD3 to form another two subsets, MDDR3 and ACD4, respectively.
Shen M., Tian S., Li Y., Li Q., Xu X., Wang J, & Hou T. (2012). Drug-likeness analysis of traditional Chinese medicines: 1. property distributions of drug-like compounds, non-drug-like compounds and natural compounds from traditional Chinese medicines. Journal of Cheminformatics, 4, 31.
Full text: Click here
Publication 2012
5
Lifespan Regulation in Podospora anserina

Strains, growth conditions and lifespan determination.
 In this study the wild-type strain s [23 (link)], the ΔPaKu70 strain [22 (link)] and the short-lived ΔPaMth1 strain were
used. All strains were grown at 27°C on P. anserina synthetic medium
(PASM) [24 (link)] under constant light. To obtain cultures of a defined
age, mycelium from freshly germinated ascospores was placed on one side of a
Petri dish containing PASM. Every 2-3 days, the growth front was marked. After
reaching the other side of the Petri dish fresh plates of PASM were inoculated
with a piece of the culture obtained from the growth front. Senescent cultures
stopped growth and displayed hyper pigmentation. For further analysis,
senescent cultures were obtained from plates shortly before growth arrest to
inoculate fresh plates for further experiments (e.g. protein isolation).


Growth rate and lifespan determination.
 Lifespan and growth rate determination
were performed with monokaryotic isolates from independent crosses. Freshly
germinated spores were placed on race tubes with PASM. The time period of
linear growth was recorded as lifespan in days. Growth rate was measured in centimetres
per day. Growth rates under oxidative stress conditions were recorded over 5 days starting
with monokaryotic isolates from independent crosses of the wild-type strain s
and the PaMth1 deletion strains on PASM plates containing 40 μM and
80 μM CuSO4, respectively.


Alternatively, growth medium was
supplemented by 0.01%, 0.02% and 0.04% hydrogen peroxide, respectively. To
protect hydrogen peroxide from disintegration, plates were kept in the dark.
For better comparability of growth rates, a wild-type strain s culture and a
deletion strain were grown on the same plate.


Deletion of PaMth1 in P. anserina. For deletion of the PaMth1 gene a vector was
generated containing a hygromycin B resistance cassette for selection in P.
anserina framed by approximately 1.0 kbps long 5' and 3' flanking sequences
of PaMth1. These regions were amplified by PCR using sequence specific
oligonucleotides introducing restriction sites for XhoI and HindIII
(5'), and PstI and XbaI (3'), respectively. After digestion of
the plasmid pKO7 with the corresponding enzymes the two digested PCR products
were cloned into this vector. The deletion vector pPaMth1KO1 was used to
transform P. anserina protoplasts of the strain ΔPaKu70. The
strains containing the recombined DNA were selected by hygromycin B resistance.


Transformation of P. anserina. Production, regeneration, and integrative
transformation of P. anserina spheroplasts was performed as described [25 (link), 26 (link)].


Isolation of mitochondria from P. anserina. Mitochondria were isolated from juvenile and senescentP. anserina cultures, respectively, according to a previously published
protocol [27 (link)] with the following modifications. Crude mitochondria
were isolated by differential centrifugation for 35 min at 15.000 g and 4° C.
The mitochondrial pellet was resuspended in 1 ml of mitochondria isolation
buffer (10 mM Tris, 1 mM EDTA, 0.33 M sucrose, pH 7.5) and layered on a 20-50%
discontinuous sucrose gradient. After centri-fugation for 1 h at 100.000 g in a
swing-out bucket rotor (TH 641) the mitochondria were banding between the 50
and the 36 % sucrose step. Approximately 30 ml mitochondrial isolation buffer
without bovine serum albumin were added to the collected mitochondria fraction
and centrifuged for 15 min at 15.000 g at 4 °C. For isolation of samples for
Oxyblot analysis 100 mM DTT was added to the isolation buffer.


Oxy- and Western blot analyses.
 For Western blot analyses, total and
mitochondrial protein samples (5-20 μg of protein) were boiled for 1 min
in loading buffer [0.1 M Tris (pH 6.8), 6% SDS, 6% glycerol, 0.6 M
β-mercaptoethanol] and were separated on a 12% SDS-PAGE using a Protean
III unit (Bio-Rad, Hercules, CA, USA). Subsequently, proteins were transferred
to a PVDF membrane (Millipore, Schwalbach, Germany) by using an
electro-blotting device (Bio-Rad). Standard protocols were followed. Western
blots were probed with a PaMTH1 rabbit polyclonal antibody (α-PaMTH1).
Equal loading of total proteins was confirmed by incubation with a β-actin
mouse antibody. The loading of mitochondria was controlled by incubation with
an antibody against porin (Neurospora crassa). Detection of reacted
proteins was performed by using IRDye 680 or 800 conjugated goat anti-rabbit or
anti-mouse antibody and scanning the blots with an Odyssey infrared scanner
(Li-Cor, Lincoln, NE, USA). For Oxyblot analyses, the total protein and
mitochondrial protein samples were derivatised with di-nitro phenyl hydrazine
using an Oxyblot kit (Intergene, Millipore, Schwalbach, Germany), separated in
a 12% SDS PAGE and transferred onto a PVDF membrane (Immobilon). Blots were
incubated with a rabbit anti-DNPH antibody and an IRDye 680 or 800 conjugated
goat anti-rabbit. Reacted proteins were detected by scanning the blots with an
Odyssey infrared scanner (Li-Cor).


Kunstmann B, & Osiewacz H.D. (2009). The S-adenosylmethionine dependent O-methyltransferase PaMTH1: a longevity assurance factor protecting Podospora anserina against oxidative stress. Aging, 1(3), 328-334.
Full text: Click here
Publication 2009

Most recents protocols related to «Hydrazine»

1
Colorimetric Hydrazine Quantification
The hydrazine present in the solution was determined by the method
of Watt and Chrisp (S1). The calibration curve was plotted as follows.
A series of standard solutions were prepared by pipetting suitable
volumes of the hydrazine hydrate in colorimetric tubes and making
up to 5 mL. Then, 5 mL of color reagent (a mixture of para-(dimethylamino)
benzaldehyde (5.99 g), HCI (concentrated, 30 mL), and ethanol (300
mL) was used as a color reagent) was added and stirred for 10 min
at room temperature. Thereafter, the absorbance of the resulting solution
was measured at 460 nm, and the yields of hydrazine were estimated
from a standard curve.
Thangudu S., Wu C.H, & Hwang K.C. (2024). Photocatalytic Dinitrogen Reduction to Ammonia over Biomimetic FeMoSx Nanosheets. ACS Omega, 9(18), 20629-20635.
Full text: Click here
Publication 2024
2
Quantifying Ammonia and Hydrazine in NRR
The amounts of the produced NH3 and its N2H4 byproduct from the NRR process were determined using
the HI83300 multiparameter photometer (Hanna Instruments, Rhode Island).
Using the ASTM D1426 Nessler method33 (link),34 (link) for determination
of the concentration of NH3, 1 mL of the unreacted sample
was pipetted into the 10 mL cuvette, following which 9 mL of ammonia
high-range reagent B was used to bring the cuvette contents to the
mark. After obtaining the zero background, four drops of ammonia high-range
reagent A were added to the cuvette and mixed thoroughly, and after
awaiting the color development, absorbance of the sample was measured
at 420 nm. The yield rate of ammonia (Y.R.NH3) was estimated
according to eq 1 where CNH3 is the concentration reading from the photometer in mg·L–1, V is the volume of the acid trap
in mL, t is the reduction time in seconds, and A is the area of the GCE in cm2. Ultimately,
the faradaic efficiency (FE) of the NRR process was calculated based
on eq 2 where CNH3 and V are described above, F is the faradaic constant, MwNH3 is the molecular
weight of ammonia (17 g mol–1), and Q is the accumulated charge of the electrode during the NRR process.
For quantification of the hydrazine concentration after the NRR
process, the D1385 p-dimethylamino-benzaldehyde method
was used. Typically, two 10 mL cuvettes were filled with the unreacted
sample and deionized water, respectively. To each cuvette, 12 drops
of the hydrazine reagent were added, after which the cuvette containing
the deionized water was used for zero background correction, and the
sample containing the hydrazine reagent was used for measurement of
absorbance at 466 nm. Similar equations were used to determine the
amount of the byproduct N2H4, whereby CN2H4 was the concentration
reading from the photometer in μg·L–1 and MwN2H4 was the molecular weight
of hydrazine (32 g mol–1).
Matsoso J.B., Antonatos N., Dekanovský L., Lontio Fomekong R., Elliot J.D., Gianolio D., Mazánek V., Journet C, & Sofer Z. (2024). Enhancing Nitrogen Reduction Reaction through Formation of 2D/2D Hybrid Heterostructures of MoS2@rGO. ACS Applied Materials & Interfaces, 16(19), 24514-24524.
Full text: Click here
Publication 2024
3
Synthesis of Hydrazine Dicarboxylate Precursor
Not available on PMC !

Example 2

[Figure (not displayed)]

Di-tert-butyl 1,2-bis(2-(tert-butoxy)-2-oxoethyl)hydrazine-1,2-dicarboxylate (6.51 g, 14.14 mmol) in 1,4-dioxane (40 ml) was added HCl (12 M, 10 ml). The mixture was stirred for 30 min, diluted with dioxane (20 ml) and toluene (40 ml), evaporated and co-evaporated with dioxane (20 ml) and toluene (40 ml) to dryness to afford the crude title product for the next step without further production (2.15 g, 103% yield, ˜93% pure). MS ESI m/z calcd for C4H9N2O4 [M+H]+ 149.05, found 149.40.

US11873281B2. Conjugates of cell binding molecules with cytotoxic agents (2024-01-16). HANGZHOU DAC BIOTECH CO., LTD. [CN], None [US], None [CN], None [CN]. Inventors: R. Yongxin Zhao [US], Yue Zhang [CN], Yourang Ma [CN].
Full text: Click here
Patent 2024
Acids Anabolism Dioxanes hydrazine tert-butoxy TERT protein, human Toluene
4
Benzothiophene-3-carboxaldehyde Hydrazine Synthesis
Not available on PMC !
Benzothiophene-3-carboxaldehyde (1 mmol) was reacted with 4-bromophenyl hydrazine hydrochloride (1.2 mmol) in 20 ml of absolute ethanol in the presence of 0. : 109.38; 113.78; 123.00; 124.61; 125.05; 125.12; 128.53; 131.79; 131.87; 134.90; 135.62; 140.17; 144.63 (azomethine C) ; ESI MS m/z 331(M+,%100),333(M+2, %90).
Gürsoy Ş., Çaka Z., Faydalı N., Shirinzadeh H., & Dilek E. (2024). Exploring Novel Schiff Base Compounds Derived from Benzothiophene-3- carboxaldehyde Hydrazones: In vitro and In silico Evaluation as Potential Inhibitors of Cholinesterases and Carbonic Anhydrases I-II. Erzincan Üniversitesi Fen Bilimleri Enstitüsü Dergisi, 17(1), 174-195.
Publication 2024
5
Synthesis of Bromoaroyl Hydrazine Acetic Acid
Not available on PMC !

Example 3

[Figure (not displayed)]

To a solution of 2,2′-(hydrazine-1,2-diyl)diacetic acid (1.10 g, 7.43 mmol) in the mixture of THF (50 ml) and NaH2PO4 (0.1 M, 80 ml, pH 6.0) was added (E)-3-bromoacryloyl bromide (5.01 g, 23.60 mmol). The mixture was stirred for 6 h, concentrated and purified on SiO2 column eluted with H2O/CH3CN (1:9) containing 3% formic acid to afford the title compound (2.35 g, 77% yield, ˜93% pure). MS ESI m/z calcd for C10H11Br2N2O6 [M+H]+ 412.89, found 413.50.

US11873281B2. Conjugates of cell binding molecules with cytotoxic agents (2024-01-16). HANGZHOU DAC BIOTECH CO., LTD. [CN], None [US], None [CN], None [CN]. Inventors: R. Yongxin Zhao [US], Yue Zhang [CN], Yourang Ma [CN].
Full text: Click here
Patent 2024
Acids Anabolism Bromides formic acid hydrazine

Top products related to «Hydrazine»

1
Hydrazine hydrate by Merck Group
Sourced in United States, Germany, India, France, China
Hydrazine hydrate is a colorless, crystalline compound. It is the hydrate form of hydrazine, a reducing agent used in various industrial applications. Hydrazine hydrate has a chemical formula of N₂H₄·H₂O and is soluble in water and polar organic solvents.
2
Hydrazine by Merck Group
Sourced in United States, Germany, United Kingdom, India
Hydrazine is a chemical compound with the formula N2H4. It is a colorless, flammable liquid with a distinctive pungent odor. Hydrazine is commonly used as a reducing agent, fuel, and in the synthesis of other chemical compounds.
3
Hydrazine monohydrate by Merck Group
Sourced in United States, Germany, France, Canada, India
Hydrazine monohydrate is a chemical compound with the formula N2H4·H2O. It is a colorless, crystalline solid with a distinctive ammonia-like odor. Hydrazine monohydrate is commonly used as a reducing agent, a fuel component, and in the manufacture of various chemicals and pharmaceuticals.
4
Sodium hydroxide (naoh) by Merck Group
Sourced in Germany, United States, India, United Kingdom, Italy, China, Spain, France, Australia, Canada, Poland, Switzerland, Singapore, Belgium, Sao Tome and Principe, Ireland, Sweden, Brazil, Israel, Mexico, Macao, Chile, Japan, Hungary, Malaysia, Denmark, Portugal, Indonesia, Netherlands, Czechia, Finland, Austria, Romania, Pakistan, Cameroon, Egypt, Greece, Bulgaria, Norway, Colombia, New Zealand, Lithuania
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.
5
Ethanol by Merck Group
Sourced in Germany, United States, United Kingdom, Italy, India, France, China, Australia, Spain, Canada, Switzerland, Japan, Brazil, Poland, Sao Tome and Principe, Singapore, Chile, Malaysia, Belgium, Macao, Mexico, Ireland, Sweden, Indonesia, Pakistan, Romania, Czechia, Denmark, Hungary, Egypt, Israel, Portugal, Taiwan, Province of China, Austria, Thailand
Ethanol is a clear, colorless liquid chemical compound commonly used in laboratory settings. It is a key component in various scientific applications, serving as a solvent, disinfectant, and fuel source. Ethanol has a molecular formula of C2H6O and a range of industrial and research uses.
6
Hydrochloric acid (hcl) by Merck Group
Sourced in Germany, United States, United Kingdom, India, Italy, France, Spain, Australia, China, Poland, Switzerland, Canada, Ireland, Japan, Singapore, Sao Tome and Principe, Malaysia, Brazil, Hungary, Chile, Belgium, Denmark, Macao, Mexico, Sweden, Indonesia, Romania, Czechia, Egypt, Austria, Portugal, Netherlands, Greece, Panama, Kenya, Finland, Israel, Hong Kong, New Zealand, Norway
Hydrochloric acid is a commonly used laboratory reagent. It is a clear, colorless, and highly corrosive liquid with a pungent odor. Hydrochloric acid is an aqueous solution of hydrogen chloride gas.
7
Hydrazine hydrate by Sinopharm
Sourced in China
Hydrazine hydrate is a chemical compound with the formula N2H4·H2O. It is a clear, colorless liquid with a pungent odor. Hydrazine hydrate is primarily used as a reducing agent, corrosion inhibitor, and intermediate in the production of various chemicals and pharmaceuticals.
8
Methanol by Merck Group
Sourced in Germany, United States, Italy, India, United Kingdom, China, France, Poland, Spain, Switzerland, Australia, Canada, Sao Tome and Principe, Brazil, Ireland, Japan, Belgium, Portugal, Singapore, Macao, Malaysia, Czechia, Mexico, Indonesia, Chile, Denmark, Sweden, Bulgaria, Netherlands, Finland, Hungary, Austria, Israel, Norway, Egypt, Argentina, Greece, Kenya, Thailand, Pakistan
Methanol is a clear, colorless, and flammable liquid that is widely used in various industrial and laboratory applications. It serves as a solvent, fuel, and chemical intermediate. Methanol has a simple chemical formula of CH3OH and a boiling point of 64.7°C. It is a versatile compound that is widely used in the production of other chemicals, as well as in the fuel industry.
9
Hydrogen peroxide by Merck Group
Sourced in United States, Germany, India, United Kingdom, Spain, Italy, China, Canada, Poland, Switzerland, France, Brazil, Australia, Belgium, Sao Tome and Principe, Singapore, Malaysia, Japan, Macao, New Zealand, Hungary, Czechia, Nigeria, Portugal, Ireland, Cameroon, Thailand
Hydrogen peroxide is a clear, colorless liquid chemical compound with the formula H2O2. It is a common laboratory reagent used for its oxidizing properties.
10
Acetonitrile by Merck Group
Sourced in Germany, United States, Italy, India, China, United Kingdom, France, Poland, Spain, Switzerland, Australia, Canada, Brazil, Sao Tome and Principe, Ireland, Belgium, Macao, Japan, Singapore, Mexico, Austria, Czechia, Bulgaria, Hungary, Egypt, Denmark, Chile, Malaysia, Israel, Croatia, Portugal, New Zealand, Romania, Norway, Sweden, Indonesia
Acetonitrile is a colorless, volatile, flammable liquid. It is a commonly used solvent in various analytical and chemical applications, including liquid chromatography, gas chromatography, and other laboratory procedures. Acetonitrile is known for its high polarity and ability to dissolve a wide range of organic compounds.

More about "Hydrazine"