Results 311 to 320 of about 916,712 (391)

SDS Polyacrylamide Gel Electrophoresis of Proteins

Methods in molecular biology, 2003
Probably the most widely used of techniques for analyzing mixtures of proteins is SDS polyacrylamide gel electrophoresis. In this technique, proteins are reacted with the anionic detergent, sodium dodecylsulfate (SDS, or sodium lauryl sulfate) to form negatively charged complexes.
Bryan John Smith
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Agarose native gel electrophoresis of proteins

International Journal of Biological Macromolecules, 2019
We 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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Two-dimensional gel electrophoresis of proteins

Journal of Chromatography B: Biomedical Sciences and Applications, 1987
The 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.
M. Dunn
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SDS-Polyacrylamide Gel Electrophoresis of Proteins

Cold Spring Harbor Protocols, 2006
INTRODUCTIONThis 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.
David W. Russell, Joseph Sambrook
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Agarose Gel Electrophoresis of Proteins

Current Protocols in Cell Biology, 2002
AbstractThis 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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Gel Electrophoresis of Proteins and Enzymes

1976
Proteins are defined as large molecular weight substances (104 – 105) composed of amino acids coupled by the α carboxyl group of one acid and the α amino group of another forming a polypeptide:
F. Bergmann, P. P. Feret
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Rapid capillary gel electrophoresis of proteins

Journal of Chromatography A, 1993
The 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.
J. Schlösser, O. W. Reif, Ruth Freitag, Thomas Scheper, J. Fleischer, Ralf Dr. Lausch   +5 more
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Starch Gel Electrophoresis of Proteins

Methods in molecular biology, 2003
Starch 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.
Graham B. Divall
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SDS Polyacrylamide Gel Electrophoresis of Proteins

1996
Crosslinked polyacrylamide gels are formed from the polymerization of acrylamide monomer in the presence of smaller amounts of N,N'-methylene-bis-acrylamide (normally referred to as “bis-acrylamide”) (Fig. 1). Note that bis-acrylamide is essentially two acrylamide molecules linked by a methylene group and is used as a crosslinking agent.
J. Walker
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One‐Dimensional Gel Electrophoresis of Proteins

Current Protocols in Immunology, 1991
AbstractThis unit provides several methods for one‐dimensional gel electrophoresis of proteins. The basic protocol is the standard method used for gel electrophoresis under denaturing conditions. The first alternate protocol provides conditions used for nondenaturing gel electrophoresis.
Sean R. Gallagher, John A. S. Smith
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