Results 311 to 320 of about 856,230 (338)

Polyacrylamide gel electrophoresis of myelin proteins: A caution

Analytical Biochemistry, 1975
Abstract Some variables involved in the preparation of rat brain myelin proteins for polyacrylamide gel electrophoresis in buffers containing sodium dodecyl sulfate were studied. Under mild conditions of solubilization the resultant gel patterns were relatively insensitive to the β-mercaptoethanol (ME) concentration in the protein solvent used for ...
P, Morell, R C, Wiggins, M J, Gray
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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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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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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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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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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 ...
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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, preparative ...
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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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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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Studies of DNA‐protein interactions by gel electrophoresis

ELECTROPHORESIS, 1989
AbstractThe use of gel electrophoresis in studies of nucleic acid‐protein (especially DNA‐protein) interactions has yielded much qualitative and quantitative information about a variety of such systems. The reduction in mobility of complexes relative to free DNA allows isolation and characterization of the complexes as well as determination of ...
J A, Ceglarek, A, Revzin
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