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SDS-PAGE Focusing: Preparative Aspects
Analytical Chemistry, 2007As a followup of our previous report (Zilberstein, G.; Korol, L.; Antonioli, P.; Righetti, P. G.; Bukshpan, S. Anal. Chem. 2007, 79, 821-827) on analytical SDS-PAGE focusing, a novel method is here reported for small-scale prefractionation of complex protein mixtures, for subsequent proteome analysis, based on mass separation of SDS-protein micelles ...
G. Zilberstein +3 more
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Nature Protocols, 2006
Tricine-SDS-PAGE is commonly used to separate proteins in the mass range 1-100 kDa. It is the preferred electrophoretic system for the resolution of proteins smaller than 30 kDa. The concentrations of acrylamide used in the gels are lower than in other electrophoretic systems. These lower concentrations facilitate electroblotting, which is particularly
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Tricine-SDS-PAGE is commonly used to separate proteins in the mass range 1-100 kDa. It is the preferred electrophoretic system for the resolution of proteins smaller than 30 kDa. The concentrations of acrylamide used in the gels are lower than in other electrophoretic systems. These lower concentrations facilitate electroblotting, which is particularly
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Cold Spring Harbor Protocols, 2006
INTRODUCTION Initial heating of a protein sample at 95°C in the presence of excess SDS and a thiol reagent denatures the protein mixture and disrupts disulfide bonds. Under these conditions, all reduced polypeptides bind the same amount of SDS (1.4 g of SDS per gram of polypeptide) independent of amino acid composition and sequence. The resolving power
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INTRODUCTION Initial heating of a protein sample at 95°C in the presence of excess SDS and a thiol reagent denatures the protein mixture and disrupts disulfide bonds. Under these conditions, all reduced polypeptides bind the same amount of SDS (1.4 g of SDS per gram of polypeptide) independent of amino acid composition and sequence. The resolving power
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2000
Proteins can be separated according to their molecular sizes and charges, since these factors will determine the speed at which they will travel through a gel. The SDS-PAGE method involves the denaturation of proteins with the detergent sodium dodecyl sulfate (SDS) and the use of an electric current to pull them through a polyacrylamide gel, a process ...
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Proteins can be separated according to their molecular sizes and charges, since these factors will determine the speed at which they will travel through a gel. The SDS-PAGE method involves the denaturation of proteins with the detergent sodium dodecyl sulfate (SDS) and the use of an electric current to pull them through a polyacrylamide gel, a process ...
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SDS-PAGE and Western Blotting Techniques
2003The goal of Western blotting, or more correctly, immunoblotting, is to identify with a specific antibody a particular antigen within a complex mixture of proteins that has been fractionated in a polyacrylamide gel and immobilized onto a membrane. Immunoblotting can be used to determine a number of important characteristics of protein antigens-the ...
C, Blancher, A, Jones
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Quantification of beef myofibrillar proteins by SDS-PAGE
Meat Science, 1995A semi-quantitative determination of beef myofibrillar proteins using sodium, dodecyl sulphate polyacrylamide gel electrophoresis is described. Bovine serum albumin was used as internal standard. Results indicate a linear relationship between densitometric readings after staining with Coomassie brilliant blue R(250) and protein content.
E, Claeys +3 more
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Electrophoresis of Peptides (Tricine-SDS-PAGE)
Cold Spring Harbor Protocols, 2006INTRODUCTION Typical Laemmli gel systems, which use glycine in the running buffer, are capable of resolving proteins in the molecular mass range of ~200,000 Da down to ~3000 Da. In this protocol, the standard tricine gel system is described, in which tricine is substituted for glycine.
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Determination of Protein Molecular Weights on SDS-PAGE
2018An apparent molecular weight (MW) of a protein can be determined from the migration distance of a protein complexed with a strong cationic detergent sodium dodecyl sulfate (SDS) separated on sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE).
Hiroyuki, Matsumoto +2 more
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