Difference between Gel Electrophoresis and SDS PAGE

Electrophoresis is a scientific method for separating DNA, RNA, and protein molecules depending on their electric charge and size. Some of the common electrophoresis techniques that are currently used are as follows:

  1. Gel electrophoresis (for proteins)
  2. SDS PAGE (used for proteins having molecular masses from 5 kDa to 250 kDa)
  3. Maxam-Gilbert technique (for separation of polynucleotide fragments of DNA and RNA)
  4. Immunoelectrophoresis (for antibodies and antigens)

Here, let’s look at the differences between gel electrophoresis and the SDS PAGE technique.

Table of Contents

Gel Electrophoresis

Gel electrophoresis is a technique used for separating charged molecules like RNA, DNA and proteins. This process makes use of a gel that works like a molecular sieve. It employs two types of gels – agarose and polyacrylamide. Usually, an electric field is linked to two ends of the gel in gel electrophoresis. The gel has a positive charge on one end and a negative charge on the other. The molecules RNA and DNA are negatively charged. They move through the gel pores in the direction of the positively charged end of the gel after being injected from the negative end and exposed to the electric field.

The pace of migration is determined by the size and charge of the molecule. Smaller molecules pass via the gel pores more easily and cover a long distance than bigger ones. In the gel, several bands are seen that depict various sized molecules. Special dyes like ethidium bromide are employed to visualise these bands.

It is used as a preparative procedure in several molecular biology techniques like PCR and blotting.

Also Check:Polymerase Chain Reaction Steps Notes

SDS PAGE

SDS PAGE – Sodium dodecyl sulphate-polyacrylamide gel electrophoresis

SDS PAGE is a type of gel electrophoresis used for separating macromolecular proteins of size between 5 kDa and 250 kDa. Proteins, unlike RNA and DNA, are not charged negatively and do not move toward the positive or negative end. As a result, proteins are denatured and are charged negatively prior to electrophoresis. It is accomplished by the use of a detergent known as sodium dodecyl sulphate. This technique uses polyacrylamide gel and the whole separation process is dependent on the properties of this gel.

The proteins are separated depending on the length of the polypeptide chain using the polyacrylamide gel and sodium dodecyl sulphate, which remove the influence of protein structure and charge. Moreover, this gel gives a higher resolution than agarose.

Difference between Gel Electrophoresis and SDS PAGE

Gel Electrophoresis

SDS PAGE

This technique is used for separating charged molecules like RNA, DNA and proteins.

It is a type of gel electrophoresis used for separating macromolecular proteins of size between 5 kDa and 250 kDa.

It involves both non-denaturing and denaturing techniques.

It involves denaturing of proteins.

It employs two types of gels namely agarose and polyacrylamide.

It is solely dependent on the properties of polyacrylamide gel.

In agarose gel, the run configuration is horizontal.

In polyacrylamide gel, the run configuration is vertical.

Agarose gel electrophoresis results in low resolution.

SDS PAGE gives a better resolution than agarose.

Ethidium bromide is the commonly used stain.

Silver or coomassie staining technique is used.

Explore all the important topics aligned with the updated NEET Biology syllabus, only at BYJU’S. Also check other important Difference Between Topics.

Related Topics:

Difference between Denaturation and Renaturation of DNA

Difference between mRNA, tRNA and rRNA

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Frequently Asked Questions

Q1

What is native gel electrophoresis?

When non-denaturing conditions are used to run the gels in electrophoresis, it is termed native gel electrophoresis. This means, there is an absence of denaturing agents like SDS. Thus, it does not disturb the analyte’s natural structure. Quantitative native PAGE is a high resolution and accurate type of native gel electrophoresis.
Q2

What is discontinuous electrophoresis?

Discontinuous electrophoresis is a type of PGE (polyacrylamide gel electrophoresis). Here proteins are separated in a gel that has two discontinuous parts. Usually, the one with lower concentration is layered on top of the higher concentration. The discontinuity is not just based on gel structure but also on the pH and ionic value of the buffer. SDS PAGE is also a discontinuous electrophoretic system.
Q3

What is chromatography?

Chromatography is a technique used to separate molecules of different substances present together in a cytosol or solution. Here, the solution is applied to an insoluble medium which has a different affinity for the individual molecules of the solution so that the molecules migrate through the medium at different rates.
Q4

What is the western blot technique?

In western blot technique, the proteins extracted are subjected to polyacrylamide gel electrophoresis and are then transferred onto nitrocellulose to which they bind. This nitrocellulose membrane is later probed with a specific labelled antibody and the signal is detected with autoradiography.

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