Question

Describe what kind of information can you get from SDS and native gels. how are they different from each other.

Answer 1

Ans. Sodium dodecyl sulfate polyacrylamide gel electrophoresis or SDS-PAGE and native gel electrophoresis, both these methods are used to separate proteins.

In SDS the proteins are separated on the basis of electrophoretic mobility.The protein is separated on the basis of their molecular weight. As the name suggest, SDS or sodium dodecyl sulfate is used in this method. During the process, the protein gets denatured and the reducing agent DTT (dithiothreitol) is used to break the protein disulfide bonds.

In native gel electrophoresis the proteins are separated on the basis of their size, shape, and native charge. In this method the physical shape and size of the protein plays an important role in separation along with the charge and mass of the protein. No SDS or sodium dodecyl sulfate is used in this method. No denaturants are used in this process so, recovering proteins in their native state and structure after the separation is possible. This technique can be used for preparation of purified and active proteins.