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Recovery of protein in preparative polyacrylamide gel electrophoresis
Analytical Biochemistry, 1972Abstract The recovery of protein in preparative polyacrylamide gel electrophoresis (PAGE) is a function of protein load, buffer system (pH), and gel concentration. Recovery can be substantially improved (to about 90%) by polymerization of the gel in the presence of an extraneous protein (e.g., BSA, bacitracin) but not by addition of formamide ...
G. Kapadia, A. Chrambach
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Starch‐gel electrophoresis of cereal proteins
Journal of the Science of Food and Agriculture, 1962AbstractStarch‐gel electrophoresis has been found to be a valuable tool for the investigation of cereal proteins. Eight wheat varieties have been compared using aluminium lactate buffer of low pH. Although the albumin and globulin patterns appear to be very similar, there are significant differences among the patterns arising from the gluten proteins ...
J. A. D. Ewart, G. A. H. Elton
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Separation of olive proteins by capillary gel electrophoresis
Talanta, 2012Olive proteins are not well known and there are still a lot of unknown information requiring further studies focused on the determination and characterization of these proteins. Despite the widely use of gel electrophoresis, this is the first time that capillary gel electrophoresis (CGE) is applied to separate proteins extracted from olive fruits ...
María Concepción García +4 more
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Polyacrylamide gel electrophoresis of myelin proteins: A caution
Analytical Biochemistry, 1975Abstract 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 ...
Pierre Morell +2 more
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Supramolecular Gel Electrophoresis of Acidic Native Proteins
Analytical Chemistry, 2014Amphiphilic 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 +3 more
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Gel electrophoresis in studies of protein conformation and folding
Analytical Biochemistry, 1984Electrophoresis 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 ...
David M. Goldenberg, Thomas E. Creighton
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Gel Electrophoresis of Proteins and Nucleic Acids
2017The electrophoresis technique describes migration of charged particles under the influence of an electric field. The rate of migration depends upon various factors like charge of the particle, applied electric field, and temperature and nature of the suspended medium. Gel electrophoresis is a technique in which the macromolecules like nucleic acids and
Suman Choudhary +2 more
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Agarose-acrylamide gradient gel electrophoresis of proteins
Analytical Biochemistry, 1982Abstract 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 ...
Michael A. Naughton +2 more
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SDS‐Polyacrylamide Gel Electrophoresis (SDS‐PAGE) of Proteins
, 2011Electrophoresis is a method by which a complex mixture of proteins can be separated. Sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS‐PAGE) is a technique used to move charged molecules through a gel matrix by means of an electric current ...
J. Manns
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Discontinuous gel electrophoresis of reduced membrane proteins
Biochemical and Biophysical Research Communications, 1974Summary 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.
Reinhard Rüchel +2 more
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