What is the difference between SDS PAGE and Gel Electrophoresis?

Gel electrophoresis is a method of separation in an electrical field. DNA and RNA are negatively charged molecules. Once they are packed into the gel from the negative end of the gel and put in the electric field, they move through the gel pores towards the positively charged end of the gel. The velocity of the movement hinges on the charge and size of the molecule.

Smaller molecules journey a longer distance than larger ones. The electric field is utilized for a specific time and stopped to avoid the loss of molecules and to keep the molecules at their traveled positions. In simple terms, gel electrophoresis helps distinguish molecules by size. Polyacrylamide gel electrophoresis is a technique employed to separate proteins. It is accomplished by using a detergent during SDS Page, and proteins are mixed with SDS.

SDS unfolds proteins into a linear shape and coats them with a negative charge comparative to their molecular mass. SDS Page is denaturing gel electrophoresis, and it has a serious restriction on protein analysis. Since SDS denatures proteins before separation, it does not permit the detection of enzymatic activity, protein binding interactions, and protein cofactors.

Electrophoresis is used in regard to the mass of an object. This is important in a body's protein and DNA. There are two types of electrophoresis. The first is the SDS Page. This is an abbreviation, which stands for sodium dodecyl sulfate-polyacrylamide gel electrophoresis. It is a type of gel electrophoresis that is non-selective. Many fields take advantage of this type, including forensics, biology, and biochemistry. The second type of electrophoresis is gel electrophoresis. As its name suggests, it uses gel during the process. There are two types of gels that can be used during this process, which are polyacrylamide gel and agarose gel