Results 261 to 270 of about 855,961 (311)

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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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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Two-dimensional gel electrophoresis of membrane proteins

Biochemistry, 1976
A high-resolution method for two-dimensional separation of membrane proteins is described. It involves a nondiscriminating solubilization of a membrane preparation with sodium dodecyl sulfate, followed by electrophoresis in the first dimension according to charge (by isoelectric focusing).
G F, Ames, K, Nikaido
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Gel Electrophoresis of Proteins

1998
Abstract This new edition of Gel Electrophoresis of Proteins is a completely new text, with eight of the ten chapters written by new authors. It presents the best methods, hints and tips for core procedures such as one- dimensional polyacrylamide gel electrophoresis, isoelectric focusing, two-dimensional gel electrophoresis ...
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Gel electrophoresis in studies of protein conformation and folding

Analytical Biochemistry, 1984
Electrophoresis through polyacrylamide gels is a useful method for distinguishing conformational states of proteins and analyzing the thermodynamic and kinetic properties of transitions between conformations. Although the relationship between protein conformation and electrophoretic mobility is quite complex, relative mobilities provide qualitative ...
D P, Goldenberg, T E, Creighton
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