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Fractionation hydrogen peroxide

I -- i Hydroxylamlne hydrochloride/EASILY REDUCIBLE FRACTION hUffllj-H Oxalate buffer/MODERATELY REDUCIBLE FRACTION Hydrogen peroxide/ORGANIC SULFIDIC PHASES RESIDUAL FRACTION... [Pg.30]

On the industrial scale oxygen is obtained by the fractional distillation of air. A common laboratory method for the preparation of oxygen is by the decomposition of hydrogen peroxide. H Oj, a reaction catalysed by manganese(IV) oxide ... [Pg.260]

The ammonium hydrogensulphate is returned to the electrolytic cell. A process such as this yields an aqueous solution containing about 30% hydrogen peroxide. The solution can be further concentrated, yielding ultimately pure hydrogen peroxide, by fractional distillation but the heating of concentrated hydrogen peroxide solutions requires care (see below). [Pg.278]

Dapon 35 of FMC and a similar Japanese product have been studied by gel permeation chromatography. Hydrogen peroxide acts as a regulator as well as initiator, and gives relatively large fractions of oligomers. In polymerisation between 80 and 220°C gelation occurs at 25—45% conversion (70). [Pg.86]

Although the turpentine is largely desulfurized in the stripping stage and again in the fractionation stages, many appHcations for a- and P-pinene requite further desulfurization. Such methods involve adsorption on carbon, hypochlorite treatment, hydrogen peroxide treatment, treatment with metals, or a combination of techniques (6—15). [Pg.410]

The refining process most commonly used involves treatment with hot aqueous alkaH to convert free fatty acids to soaps, followed by bleaching, usually with hydrogen peroxide, although sodium chlorite, sodium hypochlorite, and ozone have also been used. Other techniques include distillation, steam stripping, neutralization by alkaH, Hquid thermal diffusion, and the use of active adsorbents, eg, charcoal and bentonite, and solvent fractionation... [Pg.355]

The ease of oxidation varies considerably with the nature and number of ring substituents thus, although simple alkyl derivatives of pyrazine, quinoxaline and phenazine are easily oxidized by peracetic acid generated in situ from hydrogen peroxide and acetic acid, some difficulties are encountered. With unsymmetrical substrates there is inevitably the selectivity problem. Thus, methylpyrazine on oxidation with peracetic acid yields mixtures of the 1-and 4-oxides (42) and (43) (59YZ1275). In favourable circumstances, such product mixtures may be separated by fractional crystallization. Simple alkyl derivatives of quinoxalines are... [Pg.168]

Hydrogen peroxide is used by some water treatment systems to remove the disagreeable odor of sulfides in drinking water. It is available commercially in a 20.0% by mass aqueous solution. What is the mole fraction of H2Q2 ... [Pg.261]

A — 78 rC solution of (Z)-2-butenyl(diisopinocampheyl)borane (theoretically 25 mmol prepared from ( + )-a-pinenc as described in Section 1.3.3.3.3.1.1.1.) is treated with 2.0 mL (35 mmol) of acetaldehyde (added dropwise). The mixture is stirred for 3 h at — 78CC and is then treated with 18.3 mL (55 mmol) of 3 N sodium hydroxide and 7.5 mL of 30% hydrogen peroxide solution. This mixture is refluxed for 1 h. The organic phase is separated, washed with water and NaCl and dried over MgS04. The filtrate is carefully fractionated yield 75% d.r. (syn/anti) >99 1 (GC) bp Torr 90% ee. [Pg.273]

Bordwell and Boutan (BB)81 carried out extensive work on the methylsulfmyl group in 1957. It must be emphasized that they found that the preparation of pure arylmethyl sulfoxides from arylmethyl sulfides by oxidation was not a trivial matter. The frequently recommended reagent, hydrogen peroxide in acetic acid, tended to give sulfoxides contaminated with appreciable quantities of sulfones, which could not be removed by fractional crystallization. Oxidation by nitric acid was found to be more satisfactory. [Pg.503]

In a falling film evaporator (4) a water-paraffin mixture is distilled off and completely pumped back to the reactor. The resulting product is separated into a 60% sulfuric acid fraction and paraffin-containing alkanesulfonic acid (5), which is bleached by hydrogen peroxide (6). In a stirred vessel (7) the alkanesulfonic acid is neutralized by 50% sodium hydroxide solution until the pH is exactly 7. The composition of the neutralized product is also given in Table 2. [Pg.148]

Uncertainties in Photochemical Models. The ability of photochemical models to accurately predict HO concentrations is undoubtedly more reliable in clean vs. polluted air, since the number of processes that affect [HO ] and [H02 ] is much greater in the presence of NMHC. Logan et al (58) have obtained simplified equations for [HO ] and [HO2 ] for conditions where NMHC chemistry can be ignored. The equation for HO concentration is given in Equation E6. The first term in the numerator refers to the fraction of excited oxygen atoms formed in R1 that react to form HO J refers to the photodissociation of hydrogen peroxide to form 2 HO molecules other rate constants refer to numbered reactions above. [Pg.92]

C12-0037. A saturated solution of hydrogen peroxide in water contains 30.% by mass H2 O2 and has a density of 1.11 g/mL. Calculate the mole fractions, molarity, and molality of this solution. [Pg.880]

Figure 15.9 The results of capture ELISA on native RNase A and formalin-treated RNase A. Right panel, native RNase A (curve 1) and unfractionated formalin-treated RNase A (curve 2). Left panel, individual fractions of formalin-treated RNase A monomer (curve 3), dimmer (curve 4), trimer (curve 5), tetramer (curve 6), and a mixture of oligomers with >5 cross-linked proteins (curve 7). The ELISA plate wells were coated with monoclonal antibody against bovine pancreatic RNase A (1 pg/mL) overnight at 4°C and then blocked with bovine serum albumin. The wells were incubated for lh at 37°C in the presence of various concentrations of antigen in lOOpL of PBS. After washing, each plate well received a 1 4000 dilution of horseradish peroxidase conjugated rabbit polyclonal anti-RNase A antibody followed by incubation at ambient temperature for lh. After washing, detection was achieved using a mixture of 2,2,-azino-di-(3-ethylbenzthiazoline-6-sulphonate) and hydrogen peroxide. Absorbance was monitored at 405 nm. See Rait etal.11 for details. Figure 15.9 The results of capture ELISA on native RNase A and formalin-treated RNase A. Right panel, native RNase A (curve 1) and unfractionated formalin-treated RNase A (curve 2). Left panel, individual fractions of formalin-treated RNase A monomer (curve 3), dimmer (curve 4), trimer (curve 5), tetramer (curve 6), and a mixture of oligomers with >5 cross-linked proteins (curve 7). The ELISA plate wells were coated with monoclonal antibody against bovine pancreatic RNase A (1 pg/mL) overnight at 4°C and then blocked with bovine serum albumin. The wells were incubated for lh at 37°C in the presence of various concentrations of antigen in lOOpL of PBS. After washing, each plate well received a 1 4000 dilution of horseradish peroxidase conjugated rabbit polyclonal anti-RNase A antibody followed by incubation at ambient temperature for lh. After washing, detection was achieved using a mixture of 2,2,-azino-di-(3-ethylbenzthiazoline-6-sulphonate) and hydrogen peroxide. Absorbance was monitored at 405 nm. See Rait etal.11 for details.

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