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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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2018
The discontinuous polyacrylamide gel electrophoresis system devised by Laemmli (Nature 227:680-685, 1970) has not only been used in numerous laboratories but has also been modified in several ways since its birth. In our laboratories, we use a modified Laemmli SDS-PAGE system for following protein purification as well as for analysis of certain protein-
Lars, Backman, Karina, Persson
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The discontinuous polyacrylamide gel electrophoresis system devised by Laemmli (Nature 227:680-685, 1970) has not only been used in numerous laboratories but has also been modified in several ways since its birth. In our laboratories, we use a modified Laemmli SDS-PAGE system for following protein purification as well as for analysis of certain protein-
Lars, Backman, Karina, Persson
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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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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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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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Protein Determination by SDS-PAGE
SDS-PAGE is the abbreviated form of sodium-dodecyl sulphatepolyacrylamide gel electrophoresis. It is a commonly used gel electrophoresis for the qualitative estimation of proteins. It is based on the principle that treatment of protein with SDS, an anionic detergent, causes a constant negative charge throughout the protein surface.openaire +1 more source