Question

What is the function/ capability of that type of gel and explain the basis for its ability to function in that capasity for these three types of gel electrophoresis:

A) agarose gels

B) Acrylamide (non-denaturing or native) gels

C) SDS-PAGE (denaturing) gels

thank you!

Answer 1

Gel electrophoresis is a method used in the laboratory for the separation of a mixture of molecules of DNA, RNA, PROTEIN according to molecular size. The molecules are pushed by an electrical field through a gel that contains small pores.

Agarose gel electrophoresis:- It is used to separate a mixture of DNA or protein in the matrix of agarose. Agarose is one of the main components of agar. The protein may be separated by size or charge and DNA by fragments by length. Agarose gel has a large pore size and good gel strength, making it suitable for making medium for electrophoresis of DNA and large protein molecules.

Acrylamide( non denaturing or native) gels:- Native polyacrylamide gel electrophoresis is performed using 6% acrylamide gels in Tris‐boric‐EDTA (8.9mM Tris base, 8.9mM boric acid, 0.2mM Na2EDTA) buffer, pH 8. They are gels without denaturant (urea) to prevent denaturation of DNA molecule during electrophoresis. non-denaturing gels, analyze proteins that are still in their folded state. Thus, the electrophoretic mobility depends not only on the charge-to-mass ratio but also on the physical shape and size of the protein.

SDS-PAGE (denaturing) gels:- SDS-PAGE (sodium dodecyl sulfate-polyacrylamide gel electrophoresis), the use of sodium dodecyl sulfate (SDS, also known as sodium lauryl sulfate).SDS-PAGE is an electrophoresis method that allows protein separation by mass.SDS-PAGE separates proteins primarily by mass because the ionic detergent SDS denatures and binds to proteins to make them uniformly negatively charged. Thus, when a current is applied, all SDS-bound proteins in a sample will migrate through the gel toward the positively charged electrode.