Buffers Butyl alcohol

The hydrated electrons were produced in a matrix consisting of triply distilled water, 0.2 M in tert. butyl alcohol (for rapid scavenging of OH-radicals), and acetate buffer, by 4—40 nsec single pulses of 15 MeV electrons. 

Buffer solution - dissolve 6.0 g ferric nitrate, Fe(N03)3.9FH20, and 0.15 g silver nitrate, AgNOj, in water and make up to 100 ml add this to a solution of 5.0 g potassium acetate in 500 ml glacial acetic acid in a 2-1 beaker and stir to mix. Add 400 ml 2-methylpropan-2-ol (tertiary butyl alcohol, (CH3)3C0H this solidifies s25.5°C, therefore it may need warming to melt before use), and stir to mix. Store in a brown glass bottle. 

Proteases have also been successfully used in ionic liquids. Papain mediated the enantioselective hydrolysis of a number of amino acid esters in an 80 20 mixture of [BMIm][BF4] and water [68]. The reaction rate was approx. 50% of that in aqueous buffer and equal to that in aqueous mixtures containing 70- 80% of solvents such as acetonitrile or tert-butyl alcohol. 

The spectra of dry films of intact ghosts prepared by lysis in 20 millios-molal phosphate buffer (21) and of ghost protein prepared by cold butyl alcohol extraction (51) are shown in Figure 6. In both cases the amide I band occurs at 1651 cm. 1 and shows no shoulder near 1630 cm. 1, characteristic of fl structure. The amide II band is also unaffected by removal of lipid and occurs at 1540 cm."1. As expected, extraction of lipid results in removal of the band at 1737 cm. 1 assigned to lipid ester carbonyl stretch and a decrease of the band at about 1455 cm."1 arising from methylene and methyl bending. 

Andreozzi R, Caprio V, Ermellino I, Insola A, Tufano V. Ozone solubility in phosphate buffer aqueous solutions effect of temperature, tert-butyl alcohol and pH. Ind Eng Chem Res 1996 35 1467-1471. 

The cell walls of microbes contain antigenic polysaccharides. The preparation of cell walls was from freshly grown organisms and is described [23], The polysaccharides were extracted from the cells with a solution of 0.2 N HC1 and 0.2 N KC1 [24], The extract was subjected to dialysis to remove inorganic salts and with chloroform-butyl alcohol (4 1) to remove the protein by centrifugation. The filtrate was subjected to chromatography on P-60 acrylamide and the polysaccharides eluted with phosphate buffer pH 7.0. The polysaccharide was precipitated with ethyl alcohol (5 vol) from the eluate and collected [24],... 

Alcalase, a serine endopeptidase from Bacillus licheniformis and whose major component is subtUisin A (subtihsin Carlsberg)[ l has been employed to selectively saponify peptide methyl and benzyl esters (Scheme 16) in a solvent system consisting of 90% tert-butyl alcohol and 10% buffer (pH 8.2) leaving the N-terminal Fmoc group intact. A selective classical alkaline saponification of methyl esters would have been impossible due to the base sensitivity of the Fmoc group. 

One of the largest uses for lipases174 may be in the hydrolysis and transesterification of oils and fats.175 The reactions with enzymes are much gentler than the ones used today, such as hydrolysis of a fat or oil in water at 150 260 C for 3-24 h. They are also less capital-intensive. Lipases can be used for the hydrolysis and subsequent reesterification with butyl alcohol of olive and rapeseed oils in 100% conversion. An Aspergillus lipase hydrolyzed various fats and oils in the presence of an aqueous buffer in 90-99% yields in 2-24 h.176 Much of the lipase remained in the emulsion at... 

Sample preparation Add 20 pL 30 p,g/mL cyheptamide in MeOH to a tube and evaporate the MeOH, add 1 mL plasma, add 2 mL buffer, add 20 mL chloroform t-butyl alcohol 95 5, shake horizontally at 180 organic layer and evaporate it to dryness under reduced pressime at 65 , reconstitute the residue in 50 pL mobile phase, vortex, iigect a 10 p,L aliquot. (Buffer was 50 mL 200 mM Na2HP04.7H20 + 6.3 mL 400 mM NaOH, pH 11.2.)... 

The decomposition products in irradiated solutions of polymyxin and in their hydrolysates were identified by paper electrophoresis in a pyridine-acetate buffer solution (pH 5.7, 1200 volts) and by paper chromatography using the systems butyl alcohol-acetic acid-water (4 1 5) and phenol-ethyl alcohol-water (2 1 1, in an NH3 atmosphere). For detection, ninhydrin and 2,4-dinitrophenyl hydrazine were used. 

The enantiomers of azepinoindole and its 7V-desmethyl metabolites were well resolved on a 8-cyclodextrin-modified silica column (A = 231 run). A 1/99 r-butyl alcohol/water (10 mM sodium phosphate buffer at pH 7 with 15 mM jS-cyclodextrin and 2 mM triethylamine) mobile phase was used to generate the chiral separation. The assay calibration range covered 100-500 ng/mL. Peaks were somewhat tailed. Elution was complete in 25 min [584]. 

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