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Tiselius

A. W. K. Tiselius (Uppsala) electrophoresis and adsorption analysis, especially for discoveries concerning the complex nature of the serum proteins. [Pg.1297]

Fendler, J. H. (1982). Membrane Mimetic Chemistry. John Wiley, New York Fredga, A. (1944). In The Svedberg Memorial Volume (ed. A. Tiselius and K. O. [Pg.136]

Modes of Operation The classical modes of operation of chromatography as enunciated by Tiselius [Kolloid Z., 105, 101 (1943)] are elution chromatography, frontal analysis, and displacement development. Basic features of these techniques are illustrated in Fig. 16-29. Often, each of the different modes can be implemented with the same equipment and stationary phase. The results are, however, quite different in the three cases. [Pg.38]

The idea of annular chromatography was first mentioned by A.J.P. Martin [4] in 1949 where he summarized a discussion with his colleagues Prof. Tiselius and Dr. Synge. In his summary Martin writes ... [Pg.234]

Martin further mentioned that the scheme he described has already been tried out by Dr. Wadman of the University of Bristol. Wadman, however, never published any results of his very first work on annular chromatography. Martin and Synge won a joint Nobel price in chemistry for their work in partition chromatography, Tiselius won a Nobel price in chemistry for his work in electrophoreses. [Pg.235]

Charcoal and Activated Carbon Tiselius used charcoal for the frontal analysis of sugars, amino acids and other substances. Charcoal absorbs strongly aromatic substances, such as amino acids, which may be explained by virtue of the fact that the carbon-carbon spacings in graphite are almost of the same order as those present in benzene. Charcoal is also employed for the adsorption of fatty acids. [Pg.415]

Moving-boundary electrophoretic techniques, originally demonstrated by Tiselius in 1937, employ a U-tube with the sample occupying the lower part of the U and the two limbs being carefully filled with a buffered electrolyte so as to maintain sharp boundaries with the sample. Electrodes are immersed in the electrolyte and direct current passed between them. The rate of migration of the sample in the electric field is measured by observing the movement of the boundary as a function of time. For colourless samples, differences in refractive index may be used to detect the boundary. Such moving-boundary techniques are used mainly in either studies of the physical characteristics of molecules or bulk preparative processes. [Pg.133]

The third test of protein homogeneity, developments from which remain in common use, was that of electrophoresis. Arne Tiselius had been a research assistant in Svedberg s laboratory. From 1925 he pioneered the application of electrophoresis to the analysis and separation of protein mixtures, showing with dialyzed serum differences in mobility of the protein components and the presence of three classes of globulins, a, B, and y. [Pg.171]

Electrophoretic separations in the purely liquid phase, as used by Tiselius, were complicated by the need to keep stable boundary conditions. Problems arose from convectional and gravitational mixing. In the 1950s various attempts were made to increase the stability and thus the reproducibility of the procedure by using filter paper, or more effec-... [Pg.171]

Svedberg, T. Pederson, K.O. (1940). The Ultracentrifuge. Oxford University Press. Tiselius, A. (1947). Adsorption analysis of amino-acids. Adv. Protein Chem. 3, 67-93. Young, E.G. (1963). Occurrence, Classification, Preparation and Analysis of Proteins. In Comprehensive Biochemistry (Florkin, M. Stotz, E.H., Eds.), Vol. 7, pp. 1-55. Elsevier, Amsterdam. [Pg.189]

The origins, principles, methods, and modes of capillary electrophoresis (CE) are discussed. Massive application of electrophoresis methods started after Tiselius s moving boundary method that was optimized by the use of paper or a gel as a semiconducting medium. The applications of paper and gel electrophoresis were situated mostly in the biochemical environment for the analysis of proteins, amino... [Pg.9]

With the study of the migration of hydrogenium ions (H ) in a phenolphthalein gel by Lodge in 1886 and the description of the migration of ions in saline solutions by Kohlraush in 1897, a basis was set for the development of a new separation technique that we know today as electrophoresis. Indeed, several authors applied the concepts introduced by Lodge and Kohlraush in their methods and when Arne Tiselius reported the separation of different serum proteins in 1937, the approach called electrophoresis was recognized as a potential analytical technique. Tiselius received the Nobel Prize in Chemistry for the introduction of the method called moving boundary electrophoresis. ... [Pg.10]

Arne WK. Tiselius Sweden electrophoresis and serum proteins... [Pg.409]

The equation for the description of equilibrium in zone electrophoresis was first introduced by Tiselius (6). For interactions that produce 1 1 stoichiometry ... [Pg.191]

A Tiselius. Moving boundary method of studying the electrophoresis of proteins. Nova Acta Reg Soc Uppsal Ser IV 7 1-107, 1930. [Pg.217]


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Arne Tiselius

Electrophoresis Tiselius method

Electrophoresis Tiselius moving-boundary

Mixtures Arne Tiselius

Tiselius apparatus

Tiselius apparatus separations

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