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Purification, and Analysis

Purification. Distillation is most commonly used for purifying solvents. Solvents with different vapor pressures can be separated from one another by fractional distillation. Azeotropic mixtures can be separated by extractive or azeotropic distillation (e.g., addition of benzene to a water-ethanol mixture), by chemical reaction of a component (e.g., addition of acetic anhydride to an ethanol-ethyl acetate mixture), or by altering the pressure during distillation. [Pg.318]

Further methods for purifying solvents include freezing out water from solvents that are partially miscible with water, extracting water-soluble constituents from water-immiscible solvents by shaking with water, and the use of adsorbents (e.g., activated charcoal). [Pg.318]

Analysis. Solvent purity is assessed by means of gas chromatography [14.175]-[14.181], physical properties, water content, evaporation residue, and acid, saponification, and hydroxyl numbers [14.182]. Color and smell are also evaluated. [Pg.318]

Standardized tests are employed in the analysis of solvents (see Table 20). [Pg.318]

A very important use of MS in combinatorial chemistry is in quality control of combinatorial libraries. As much as possible, we would like to have pure compounds generated in high yield, with no side reactions or by-products. We also need to verify that every component actually exists in a library (i.c.. that no reactions failed). Only MS provides the sensitivity and versatility to perform this checking with both solid-pha.se and solution-phase libraries [Pg.52]


Biomolecule Separations. Advances in chemical separation techniques such as capillary zone electrophoresis (cze) and sedimentation field flow fractionation (sfff) allow for the isolation of nanogram quantities of amino acids and proteins, as weU as the characterization of large biomolecules (63—68) (see Biopolymers, analytical techniques). The two aforementioned techniques, as weU as chromatography and centrifugation, ate all based upon the differential migration of materials. Trends in the area of separations are toward the manipulation of smaller sample volumes, more rapid purification and analysis of materials, higher resolution of complex mixtures, milder conditions, and higher recovery (69). [Pg.396]

The purification and analysis of individual amino acids from complex mixtures was once a very difficult process. Today, however, the biochemist has a wide variety of methods available for the separation and analysis of amino acids, or for that matter, any of the other biological molecules and macromolecules we... [Pg.101]

E. Davoli, R. Fanelli and R. Bagnati, Purification and analysis of dmg residues in urine samples by on-line immunoaffinity cliromatography/bigh-performance liquid cliro-matography/continuos-flow fast atom bombardment mass spectrometry . Anal. Chem. 65 2679-2685 (1993). [Pg.298]

Londo, T., Lynch, R, Kehoe, T., Meys, M., and Gordon, N., Accelerated recombinant protein purification process development. Automated, robotics-based intergration of chromatographic purification and analysis, /. Chromatogr. A, 798, 73, 1998. [Pg.308]

Rupp GM, Locker J. Purification and analysis of RNA from paraffin-embedded tissues. BioTechniques 1988 6 56-60. [Pg.66]

Experiment 22 Synthesis, Purification and Analysis of an Organic Compound... [Pg.332]

It was further found that the methods separate well the dyes and impurities, as demonstrated on the preparative chromatographic profile of Reactive orange 16 in Fig. 3.115. It was concluded from the results that the method can be used in the future for the purification and analysis of a wide variety of sulphonated azo dyes [171],... [Pg.498]

Kessel D, Thompson P (1987) Purification and analysis of hematoporphyrin and hematoporphyrin derivative by gel exclusion and reverse-phase chromatography. Photochem Photobiol 46 1023-1025. [Pg.103]

Upon purification of the XDH from C. purinolyticum, a separate Se-labeled peak appeared eluting from a DEAE sepharose column. This second peak also appeared to contain a flavin based on UV-visible spectrum. This peak did not use xanthine as a substrate for the reduction of artificial electron acceptors (2,6 dichlor-oindophenol, DCIP), and based on this altered specificity this fraction was further studied. Subsequent purification and analysis showed the enzyme complex consisted of four subunits, and contained molybdenum, iron selenium, and FAD. The most unique property of this enzyme lies in its substrate specificity. Purine, hypoxanthine (6-OH purine), and 2-OH purine were all found to serve as reductants in the presence of DCIP, yet xanthine was not a substrate at any concentration tested. The enzyme was named purine hydroxylase to differentiate it from similar enzymes that use xanthine as a substrate. To date, this is the only enzyme in the molybdenum hydroxylase family (including aldehyde oxidoreductases) that does not hydroxylate the 8-position of the purine ring. This unique substrate specificity, coupled with the studies of Andreesen on purine fermentation pathways, suggests that xanthine is the key intermediate that is broken down in a selenium-dependent purine fermentation pathway. ... [Pg.141]

Ballihaut, G., Tastet, L., Pecheyran, C., Bouyssiere, B., Donard, O., Grimaud, R., and Lobinski, R., Biosynthesis, purification and analysis of selenomethionyl calmodulin by gel electrophoresis-laser ablation-ICP-MS and capillary HPLC-ICP-MS peptide mapping following in-gel tryptic digestion. Journal of Analytical Atomic Spectrometry 20(6), 493 99, 2005. [Pg.96]

Macromolecules such as proteins, polysaccharides, nucleic acids differ only in their physicochemical properties within the individual groups and their isolation on the basis of these differences is therefore difficult and time consuming. Considerable decreases may occur during their isolation procedure due to denaturation, cleavage, enz3rmatic hydrolysis, etc. The ability to bind other molecules reversibly is one of the most important properties of these molecules. The formation of specific and reversible complexes of biological macromolecules can serve as basis of their separation, purification and analysis by the affinity chromatography [6]. [Pg.60]

Seetharam, R. and Sharma, S.K. (1991). Purification and Analysis of Recombinant Proteins. Marcel Dekker, New York, 324. [Pg.306]

Didraga, M., Barroso, B., and Bischoff, R. (2006). Recent developments in proteoglycan purification and analysis. Curr. Pharm. Anal. 2, 323-327. [Pg.26]

R. Boyer, Concepts in Biochemistry, (1999), Brooks/Cole (Pacific Grove, CA), pp. 102-105. Protein purification and analysis. [Pg.277]

D. Voet, J. Voet, and C. Pratt, Fundamentals of Biochemistry (1999), John Wiley Sons (New York), pp. 96-107. An introduction to protein purification and analysis. [Pg.277]

Abstract Lipopolysaccharides are the major components on the surface of most Gram-negative bacteria, and recognized by immune cells as a pathogen-associated molecule. They can cause severe diseases like sepsis and therefore known as endotoxins. Lipopolysaccharide consists of lipid A, core oligosaccharide and O-antigen repeats. Lipid A is responsible for the major bioactivity of endotoxin. Because of their specific structure and amphipathic property, purification and analysis of lipopolysaccharides are difficult. In this chapter, we summarize the available approaches for extraction, purification and analysis of lipopolysaccharides. [Pg.28]


See other pages where Purification, and Analysis is mentioned: [Pg.386]    [Pg.397]    [Pg.95]    [Pg.118]    [Pg.238]    [Pg.1]    [Pg.17]    [Pg.315]    [Pg.125]    [Pg.166]    [Pg.367]    [Pg.349]    [Pg.120]    [Pg.363]    [Pg.373]    [Pg.378]    [Pg.6]    [Pg.38]    [Pg.648]    [Pg.95]    [Pg.131]    [Pg.386]    [Pg.428]    [Pg.268]    [Pg.138]    [Pg.161]    [Pg.131]    [Pg.81]    [Pg.90]    [Pg.112]    [Pg.255]   
See also in sourсe #XX -- [ Pg.572 ]




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