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Agarose native gel electrophoresis of proteins
International Journal of Biological Macromolecules, 2019We have developed an agarose-based native gel electrophoresis system that works for both acidic and basic proteins using histidine-MES buffer. This electrophoresis can be done in a flat-bed mode or a vertical mode. While in the flat-bed mode both acidic and basic proteins can be simultaneously analyzed, the vertical gel can only be used for either ...
Cynthia Li, Tsutomu Arakawa
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Agarose Gel Electrophoresis of Proteins
Current Protocols in Cell Biology, 2002AbstractThis unit describes electrophoretic separation and identification of large proteins from a complex protein mixture. Agarose gel is utilized for the electrophoretic matrix, and detection of proteins is accomplished by transfer of the proteins to a membrane that is probed with specific antibodies and chemiluminescence reagents.
Dennis M, Krizek, Margaret E, Rick
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Starch-Gel Electrophoresis of Wheat Proteins
Nature, 1960IT has been claimed that starch-gel electrophoresis may have a higher resolving power than that of the Tiselius apparatus for serum proteins1. In spite of its potential value, there have been no reports in the literature of the application of this technique to the study of wheat proteins.
G A, ELTON, J A, EWART
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Rapid capillary gel electrophoresis of proteins
Journal of Chromatography A, 1993The rapid separation of sodium dodecyl sulphate-protein complexes according to their molecular masses (M(r)) by capillary gel electrophoresis is described. Using commercial equipment, standard proteins with M(r) in the range 29,000-97,400 were resolved to the baseline in less than 2 min by utilizing a separation distance of 7 cm.
R, Lausch +5 more
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Starch Gel Electrophoresis of Proteins
2003Starch gel is one of a wide variety of supporting media that can be used for horizontal zone electrophoresis. Such gels are prepared by heating and cooling a quantity of partially hydrolyzed starch in an appropriate buffer solution. The choice of buffer is somewhat empirical and a wide variety of compositions have been used successfully.
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SDS-Polyacrylamide Gel Electrophoresis of Proteins
Cold Spring Harbor Protocols, 2006INTRODUCTIONThis protocol describes the separation of proteins by SDS-polyacrylamide gel electrophoresis. SDS is used with a reducing agent and heat to dissociate the proteins. SDS-polypeptide complexes form and migrate through the gels according to the size of the polypeptide.
Joseph, Sambrook, David W, Russell
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The interaction of proteins during gel electrophoresis
Journal of the Science of Food and Agriculture, 1966AbstractReversible polymerisation and A + B ⇌ C type reactions among proteins during zone electrophoresis may give rise to tailing, extra bands and mobility changes. One or more of these signs are likely to appear with the milder type of interaction, i.e. equilibrium constant in the range 102–108, whether the time to equilibrium is measured in hours or
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Two-dimensional gel electrophoresis of proteins
Journal of Chromatography B: Biomedical Sciences and Applications, 1987The high-resolution capacity of two-dimensional polyacrylamide gel electrophoresis (2-D PAGE) makes it an excellent tool for the analysis and characterisation of complex protein mixtures. The evolution of two-dimensional electrophoresis is briefly described.
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