Titlebook: Basic Protein and Peptide Protocols; John M. Walker Book 1994 Humana Press 1994

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Two-Dimensional Polyacrylamide Gel Electrophoresis of Proteins,2-D gel system has no serious rivals, with the possible exception of the Kaltschmidt and Wittmann (.) gel system for analyzing ribosomal proteins. Ribosomal proteins, however, may be adequately separated with NEPHGE.

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Relentlessly Pursuing Opportunities,trophoresis in gradient gels, proteins migrate until the decreasing pore size impedes further progress. Once the “pore limit” is reached, the protein banding pattern does not change appreciably with time, although migration does not cease completely. There are three main advantages of gradient gels over linear gels:

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The Lowry Method for Protein Quantitation, but its sensitivity is moderately constant from protein to protein, and it has been so widely used that Lowry protein estimations are a completely acceptable alternative to a rigorous absolute determination in almost all circumstances where protein mixtures or crude extracts are involved.

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Gradient SDS Polyacrylamide Gel Electrophoresis of Proteins,trophoresis in gradient gels, proteins migrate until the decreasing pore size impedes further progress. Once the “pore limit” is reached, the protein banding pattern does not change appreciably with time, although migration does not cease completely. There are three main advantages of gradient gels over linear gels:

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Michael Matthesius,Jan-Philipp Büchler the very high electroendosmotic flow caused by charged groups on the glass walls of the gel tubes. As a consequence, pH gradients are unstable and rarely extend above pH 8.0, leading to loss of basic proteins from 2-D maps. Gradients can be extended to pH 10 by special treatment of the glass IEF tubes (.) or by using horizontal flat-bed IEF (..).

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