Results 151 to 160 of about 168,112,797 (204)

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.
Joseph, Sambrook, David W, Russell
openaire   +2 more sources

Starch Gel Electrophoresis of Proteins

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.
openaire   +2 more sources

SDS Polyacrylamide Gel Electrophoresis of Proteins

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.
openaire   +3 more sources

The interaction of proteins during gel electrophoresis

Journal of the Science of Food and Agriculture, 1966
AbstractReversible 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
openaire   +2 more sources

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.
openaire   +2 more sources

A gel eluter for recovery of proteins separated by polyacrylamide gel electrophoresis

Analytical Biochemistry, 1982
Abstract An apparatus for the electrophoretic elution of proteins from polyacrylamide gel slices is described. The eluter is inexpensive, easy to build, and can be constructed to fit many available slab-gel apparatuses. A high yield of protein, concentrated in a small volume of solution, can be electrophoretically separated and recovered within a 24 ...
G L, Gerton, N J, Wardrip, J L, Hedrick
openaire   +2 more sources

Agarose-acrylamide gradient gel electrophoresis of proteins

Analytical Biochemistry, 1982
Abstract A new agarose-acrylamide gradient slab gel electrophoresis system is described. The preparation of this new gel has been facilitated by the use of agarose with a relatively low gelation temperature. Fractionation of marker proteins and crosslinked proteins from a subcellular cytoskeletal preparation on agarose-acrylamide gradient gels is ...
D F, Warren, M A, Naughton, L M, Fink
openaire   +2 more sources

Discontinuous gel electrophoresis of reduced membrane proteins

Biochemical and Biophysical Research Communications, 1974
Summary Fractionation of reduced membrane proteins in discontinuous sodium dodecyl sulfate gel electrophoresis is affected by reconstitution of disulfide bridges, by dissociation of dodecyl sulfate-protein complexes through sieving in the gel matrix, and by changes in mobility due to alterations in ionic environment of the sample.
C, Richter-Landsberg, R, Rüchel, T V, Waehneldt   +2 more
openaire   +2 more sources

Supramolecular Gel Electrophoresis of Acidic Native Proteins

Analytical Chemistry, 2014
Amphiphilic tris-urea molecules self-assemble into a supramolecular hydrogel in tris(hydroxymethyl)aminomethane-glycine buffer. The supramolecular hydrogel is used as a matrix for the electrophoresis of acidic native proteins, in which proteins are separated based on their isoelectric points rather than their molecular weights.
Kanako, Munenobu, Takayuki, Hase, Takanori, Oyoshi, Masamichi, Yamanaka   +3 more
openaire   +2 more sources

Resolving Proteins for Immunoblotting by Gel Electrophoresis

Cold Spring Harbor Protocols, 2018
This protocol describes Tris/glycine SDS–polyacrylamide gel electrophoresis, also known as SDS discontinuous gel electrophoresis or the Laemmli electrophoresis system. The gel-casting unit is assembled and tested to make sure that there are no leaks. Ammonium persulfate and tetramethylethylenediamine are added to the separating monomer solution, and ...
openaire   +2 more sources