Results 211 to 220 of about 576,652 (264)

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.
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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.
R, Lausch, T, Scheper, O W, Reif, J, Schlösser, J, Fleischer, R, Freitag   +5 more
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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
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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.
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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
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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
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PREPARATIVE ELECTROPHORESIS OF PROTEINS IN ACRYLAMIDE GELS*

Annals of the New York Academy of Sciences, 1964
SUMMARY(1) A simple apparatus is described for adaption of the “disc” electrophoresis techniques to a preparative procedure that permits analytic and radioactive monitoring of the effluent fractions automatically.(2) The efficiency of the procedure for separating a model system consisting of ribonuclease, trypsin, and chymotrypsin has been demonstrated.
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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
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Gel electrophoresis of proteins

1992
Abstract At one time or another during the course of protein analysis or purification, researchers are likely to make use of gel electrophoresis. All laboratories working with proteins have some capability for carrying out gel electrophoresis and all researchers have at least rudimentary knowledge of the technique. Gel electrophoresis
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The separation of membrane proteins by polyacrylamide gel electrophoresis

Biochimica et Biophysica Acta (BBA) - Biomembranes, 1971
A modified Takayama (K. Takayama, D. H. Mac Lennanan, A. Tzagoloff and C. D. Stoner, Arch. Biochem. Biophys., 114 (1966) 223.) method for acrylamide gel electrophoresis of membrane proteins is described. The method uses acetic acid, urea, phenol and mercaptoethanol as the solvent for solubilizing the membranes.
T K, Ray, G V, Marinetti
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