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Sodium Dodecyl Sulfate-Polyacrylamide Gel Electrophoresis (SDS-PAGE)

.
When protein molecules are treated with SDS, the detergent disrupts the secondary, tertiary, and quaternary structure to produce linear polypeptide chains coated with negatively charged SDS molecules.

. The detergent binds to hydrophobic regions of the denatured protein chain in a constant ratio of about 1.4 g of SDS per gram of protein.

The presence of mercaptoethanol assists in protein denaturation by reducing all disulfide bonds.

If protein samples are treated so that they have a uniform charge, electrophoretic

mobility then depends only on size.

. Thus, the molecular weights of proteins may be estimated if they are subjected to electrophoresis in the presence of a detergent, sodium dodecyl sulfate (SDS), and a disulfide bond reducing agent, mercaptoethanol.


Original text

Sodium Dodecyl Sulfate-Polyacrylamide Gel Electrophoresis (SDS-PAGE)


. When protein molecules are treated with SDS, the detergent disrupts the secondary, tertiary, and quaternary structure to produce linear polypeptide chains coated with negatively charged SDS molecules.


. The detergent binds to hydrophobic regions of the denatured protein chain in a constant ratio of about 1.4 g of SDS per gram of protein.


The presence of mercaptoethanol assists in protein denaturation by reducing all disulfide bonds.


If protein samples are treated so that they have a uniform charge, electrophoretic


mobility then depends only on size.


. Thus, the molecular weights of proteins may be estimated if they are subjected to electrophoresis in the presence of a detergent, sodium dodecyl sulfate (SDS), and a disulfide bond reducing agent, mercaptoethanol.

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