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Electrophoresis sieving

Morris, CJOR Morris, P, Molecular-Sieve Chromatography and Electrophoresis in Polyacrylamide Gels, Biochemical Journal 124, 517, 1971. [Pg.616]

Slater, GW Guo, HL, Ogston Gel Electrophoretic Sieving How Is the Fractional Volume Available to a Particle Related to Its Mobility and Diffusion Coefficient(s) , Electrophoresis 16,11, 1995. [Pg.621]

Originally, polyacrylamide was used as an anticonvective additive in slab gel electrophoresis,79 but later its molecular sieving capability was also utilized.80 Polyacrylamide is a polymer built exclusively from monomeric units, with or without cross linking.81 A chemically cross-linked network is... [Pg.400]

Chrambach, A. and Aldroubi, A., Relative efficiency of molecular sieving in solutions of four polymers, Electrophoresis, 14, 18, 1993. [Pg.420]

Hunt G. and Nashabeh W., Capillary electrophoresis sodium dodecyl sulfate nongel sieving analysis of a therapeutic recombinant monoclonal antibody a biotechnology perspective, Anal. Chem. 71, 2390,1999. [Pg.441]

Capillary SDS-Sieving Electrophoresis In the presence of a sieving matrix, mobility decreases monotonically with molecular weight for SDS-complexed proteins. This relationship is the basis of SDS-PAGE separation of proteins. [Pg.350]

Widhalm et al. (1991) reported the use of noncrosslinked polyacrylamide for protein separation in fused silica capillaries. This matrix has low viscosity and can be replaced between separations, greatly facilitating automation of the separation. A wide range of noncrosslinked polymers has been used for size-based protein separations. Noncrosslinked polymers do not form a gel, and it is inappropriate to refer to this separation as gel electrophoresis. A number of names have been used for the method. In an effort to standardize nomenclature, IUPAC has used the term capillary sieving electrophoresis. [Pg.350]

FIGURE 15.1 One-dimensional capillary electrophoresis separation of a protein homogenate prepared from the hTERT cell line. Both separations were preformed in 30 pm ID, 145 pm OD, 20 cm long capillaries at 20,000 V. (a) Micellar electrokinetic chromatography performed with a 100 mM CHES, 100 mM Tris, and 15 mM SDS buffer at pH 8.7. Sample is electro-kinetically injected with 0.25 kV for 1 s (b) Capillary sieving electrophoresis performed in 5% Dextran (513 kDa), 100 mM CHES, 100 mM Tris, 3.5 mM SDS, pH 8.7. [Pg.352]

High-efficiency separations of FQ-labeled proteins are only achieved in the presence of an anionic surfactant, such as SDS. As a result, capillary isoelectric focusing is not useful for the analysis of these proteins. Instead, we employ capillary sieving electrophoresis and micellar electrokinetic capillary chromatography for our two-dimensional electrophoresis. [Pg.360]

Hu, S., Michels, D.A.,Fazal,M.A., Ratisoontom, C., Cunningham, M.L., Dovichi,NJ. (2004). Capillary sieving electrophoresis/micellarelectrokinetic capillary chromatography for two-dimensional protein fingerprinting of single mammalian cells. Anal. Chem. 76,4044-4049. [Pg.361]

Michels, D.A., Hu, S., Damhrowitz, K.A., Eggertson, M.J., Lauterhach, K., Dovichi, NJ. (2004). Capillary sieving electrophoresis-micellar electrokinetic chromatography fully automated two-dimensional capillary electrophoresis analysis of Deinococcus radiodurans protein homogenate. Electrophoresis 25, 3098-3105. [Pg.362]

Zonal techniques are the most frequently used form of electrophoresis and involve the application of a sample as a small zone to a relatively large area of inert supporting medium which enables the subsequent detection of the separated sample zones. A wide range of supporting media have been developed either to eliminate difficulties caused by some media (e.g. the adsorptive effects of paper) or to offer additional features (e.g. the molecular sieving effects of polyacrylamide gel). [Pg.133]

Despite some refinements in the methods, the basic principles and protocols of gel electrophoresis have not changed appreciably since their introduction. Proteins are introduced into a gel matrix and separated by the combined effects of an electrical field, buffer ions, and the gel itself, which acts as a protein sieve. At the completion of the electrophoresis run, separated proteins in the gel are stained to make them visible, then analyzed qualitatively or quantitatively. The topic has been covered in numerous texts, methods articles, and reviews.1-11 In addition, apparatus and reagents for analytical and preparative gel electrophoresis are available from several suppliers. [Pg.114]

CE is a family of techniques similar to those found in conventional electrophoresis zone electrophoresis, displacement electrophoresis, isoelectric focusing (IEF), and sieving separations. Other modes of operation unique to CE include micellar electrokinetic chromatography (MEKC) and capillary electrochromatography (CEC). [Pg.164]

One of the major advantages of CE as a separation technique is the wide variety of separation modes available. Analytes can be separated on the basis of charge, molecular size or shape, pi, or hydrophobicity. The same CE instrument can be used for zone electrophoresis, IEF, sieving separations, isotachophoresis, and chromatographic techniques such as MEKC and capillary electrokinetic chromatography. This section provides a brief description of each separation mode. Zone electrophoresis, IEF, and sieving are the primary modes used for protein separations, and these will be discussed in detail in the following sections. [Pg.168]


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