Results 311 to 320 of about 864,514 (341)

Starch-gel Electrophoresis of Pig Serum Proteins

Nature, 1963
MANY variations of the original technique of Smithies1 for starch-gel electrophoresis of proteins have been developed, notably the vertical gel2, the discontinuous buffer system3, and two-dimensional applications4,5. The latter method has been used by Ashton6 in examining pig serum proteins; it has one disadvantage in being time-consuming, requiring ...
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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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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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Starch‐gel electrophoresis of cereal proteins

Journal of the Science of Food and Agriculture, 1962
AbstractStarch‐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 ...
G. A. H. Elton, J. A. D. Ewart
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Starch-gel electrophoresis of rat-serum proteins

Biochimica et Biophysica Acta, 1961
Abstract A correlation has been attempted between the multiple components of rat-serum proteins separated by starchg-gel electrophoresis and the classical fractions obtained by paper electrophoresis. To facilitate this, serum proteins separated by paper electrophoresis were run on starch and vice versa. Differences in behaviour of corresponding human
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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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Two-Dimensional Gel Electrophoresis of Total Yeast Proteins

2005
Two-dimensional gel electrophoresis (2-DE) offers the opportunity of separating several hundred proteins from a total yeast cellular extract. A detailed description is provided here of the different steps required for the separation and visualization of radiolabeled yeast proteins on high-resolution (24 cm x 20 cm) 2-D gels.
Boucherie, H., Monribot-Espagne, C.
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One‐Dimensional SDS Gel Electrophoresis of Proteins

Current Protocols in Molecular Biology, 1995
AbstractOne‐dimensional gel electrophoresis of proteins provides information about the molecular size, amount, and purity of a protein sample. Separated proteins can be recovered from polyacrylamide gels for subsequent characterization by a variety of secondary techniques, such as mass spectrometry to determine post‐translational modifications and the ...
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Two-Dimensional Polyacrylamide Gel Electrophoresis of Proteins

2003
Since O'Farrell (1) introduced the improved technique for high resolution two-dimensional polyacrylamide gel electrophoresis (2-D PAGE), it has become one of the most powerful tools for the separation and quantification of proteins from complex mixtures. The principal reason for this is that the method employs separation of denatured proteins according
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One‐Dimensional Gel Electrophoresis of Proteins

Current Protocols in Immunology, 1991
AbstractThis unit provides several methods for one‐dimensional gel electrophoresis of proteins. The basic protocol is the standard method used for gel electrophoresis under denaturing conditions. The first alternate protocol provides conditions used for nondenaturing gel electrophoresis.
Sean R. Gallagher, John A. Smith
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