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Biomolecules, separation/characterization

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]

Many biomolecules are characterized by surfaces containing extended polar regions and also extended non-polar regions. A well-known example is provided by beta-amyloid - the well-known Alzheimer protein. It has extended hydrophobic regions separated by hydrophilic regions, as discussed in Chapter 7. The hydration of extended non-polar planar surfaces may involve novel structures that are orien-tationally inverted relative to clathrate-hke hydration shells, where unsatisfied HBs are directed towards the hydrophobic surface. We have discussed these two geometric arrangements in the appendix to this chapter (Appendix 8.A). [Pg.123]

The book is separated into five major sections One short section on general aspects of spectroscopy, molecular biology and data evaluation is followed by an introduction into the NMR of commonly encountered classes of biomolecules. Thereafter, recent developments in spectroscopic techniques are highlighted. The next section describes experiments and practical aspects useful for the characterization of protein-ligand interactions. The final section presents an account on strategies for drug development using NMR written by experts from pharmaceutical industry. [Pg.491]

In the last two decades, CE has advanced significantly as a technique for biomolecular characterization. It has not only passed the transition from a laboratory curiosity to a mature instrument-based method for micro-scale separation, but has also emerged as an indispensable tool in the biotech and pharmaceutical industries (Chapter 14). CE has become a method of choice in R D for molecular characterization, and in QC for release of therapeutic biomolecules. In the biopharmaceutical industry, more and more CE methods have been validated to meet ICH requirements. To demonstrate the influence of CE in RScD for method development and in manufacturing for the release of therapeutic proteins and antibodies, examples from the pharmaceutical industry are provided in Chapter 14. [Pg.6]

Chromatographic approaches have been also used to separate nanoparticles from samples coupled to different detectors, such as ICP-MS, MS, DLS. The best known technique for size separation is size exclusion chromatography (SEC). A size exclusion column is packed with porous beads, as the stationary phase, which retain particles, depending on their size and shape. This method has been applied to the size characterization of quantum dots, single-walled carbon nanotubes, and polystyrene nanoparticles [168, 169]. Another approach is hydro-dynamic chromatography (HDC), which separates particles based on their hydro-dynamic radius. HDC has been connected to the most common UV-Vis detector for the size characterization of nanoparticles, colloidal suspensions, and biomolecules [170-172]. [Pg.27]

In the last years, the use of comprehensive liquid chromatography has been greatly increased and it has been widely used to separate and characterize various complex samples, such as biomolecules [10-15], polymers [16,17], lipids [18-21], essential oils [22], acidic and phenolic compounds [23-28], pharmaceuticals and traditional medicines [29-31], etc. Comprehensive LC has been reviewed by several authors [32-37]. [Pg.103]

CAE employing antibodies or antibody-related substances is currently referred to as immunoaf-hnity capillary electrophoresis (lACE), and is emerging as a powerful tool for the identification and characterization of biomolecules found in low abundance in complex matrices that can be used as biomarkers, which are essential for pharmaceutical and clinical research [166]. Besides the heterogeneous mode utilizing immobilized antibodies as described above, lACE can be performed in homogeneous format where both the analyte and the antibody are in a liquid phase. Two different approaches are available competitive and noncompetitive immunoassay. The noncompetitive immunoassay is performed by incubating the sample with a known excess of a labeled antibody prior to the separation by CE. The labeled antibodies that are bound to the analyte (the immuno-complex) are then separated from the nonbound labeled antibody on the basis of their different electrophoretic mobility. The quantification of the analyte is then performed on the basis of the peak area of the nonbonded antibody. [Pg.186]

The molecular details of a biochemical process cannot be fully elucidated until the reacting molecules have been isolated and characterized. Therefore, our understanding of biochemical principles has increased at about the same pace as the development of techniques for the separation and identification of biomolecules. Chromatography has been and will continue to be the most effective technique for isolating and purifying all types of biomolecules. In addition, it is widely used as an analytical tool to measure quantitative properties. [Pg.59]

L. Stryer, Biochemistry, 4th ed. (1995), Freeman (New York), pp. 51-52. Ultracentrilu gation for separation and characterization of biomolecules. [Pg.208]

Electrophoresis makes use of differences in the electrophoretic mobility of electrically charged particles (biomolecules, micro-organisms etc.) as a means to separate them. For this purpose, a homogeneous, rectified electrical field is used. Thanks to the excellent resolution and mild operating conditions, this is currently the best analytical method for protein separation, purification and characterization. It is also used as a preparative separation method which allows a few grams per hour to be purified. [Pg.169]

A large number of variants of gel electrophoresis are used in bioanalytical analysis to allow separation and characterization of biomolecules, in particular nucleic acids (DNA, RNA) and proteins. The term gel refers to the matrix used to separate biomolecules, and in most cases is a cross-linked polymer. [Pg.166]

While straight MS analysis can yield important information in terms of identification, characterization and quantification of biomolecules, it becomes a much more powerful tool with further MS or when combined with other separation technologies. As noted earlier, these approaches include MS/MS, GC-MS, LC-MS and CE-MS. These methods have been extensively exploited in virtually all aspects of bioanalysis, and while fundamentally useful for peptide and protein analysis, these methods have also been used in the analysis of lipids, nucleic acids and a wide range of small molecules and drugs. The range of applications is obviously outside the scope of a book like this, but some indications of the uses of each of these techniques are given below. [Pg.194]

Since the introduction of metal-ion affinity sorbents for the fractionation of proteins [1], the method became popular for the purification of a wide variety of biomolecules. Metal-ion affinity sorbents are also widely used for the immobilization of enzymes. At present, IMAC is a powerful method for separation of phosphorylated macromolecules, particularly proteins and peptides. The significance of techniques for separation and characterization of phosphorylated biomolecules is now increasing, because phosphorylation modulates enzyme activities and mediates cell membrane permeability, molecular transport, and secretion. Phosphorylated peptides can be separated from a peptide mixture on IDA-Sepharose with Fe " ions (Fig. 2). The majority of peptides pass freely through an IMAC column, whereas acidic peptides, including phosphorylated ones, are retained and can be released by a pH gradient. [Pg.350]

Separation and Characterization of Biomolecules Based on Macroscopic Properties... [Pg.109]


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See also in sourсe #XX -- [ Pg.109 , Pg.110 , Pg.111 , Pg.112 , Pg.113 ]




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