Native page electrophoresis vs sds page electrophoresis
Answers
The difference between SDS-PAGE, Native PAGE, and Isoelectric focusing:
The difference between SDS-PAGE, Native PAGE, and Isoelectric focusing:In SDS PAGE, the protein being separated is first subjected to a detergent, known as SDS (sodium dodecyl sulfate). This detergent denatures the protein. The 3D structure of the protein will not be revealed after separation. Samples move in PAGE gel, only on basis of size.
The difference between SDS-PAGE, Native PAGE, and Isoelectric focusing:In SDS PAGE, the protein being separated is first subjected to a detergent, known as SDS (sodium dodecyl sulfate). This detergent denatures the protein. The 3D structure of the protein will not be revealed after separation. Samples move in PAGE gel, only on basis of size.In Native PAGE, the protein being separated is not subjected to any detergent. This means that the protein remains as it is. It is being separated from its native form intact. The 3D structure of the protein can be revealed after separation. Here the samples move on the basis of size and charge.
The difference between SDS-PAGE, Native PAGE, and Isoelectric focusing:In SDS PAGE, the protein being separated is first subjected to a detergent, known as SDS (sodium dodecyl sulfate). This detergent denatures the protein. The 3D structure of the protein will not be revealed after separation. Samples move in PAGE gel, only on basis of size.In Native PAGE, the protein being separated is not subjected to any detergent. This means that the protein remains as it is. It is being separated from its native form intact. The 3D structure of the protein can be revealed after separation. Here the samples move on the basis of size and charge.In isoelectric focusing, the proteins are separated on the basis of their isoelectric point. The net charge on the protein can also be determined using this technique. Samples move in the gel on the basis of size, charge and isoelectric point.
The difference between SDS-PAGE, Native PAGE, and Isoelectric focusing:In SDS PAGE, the protein being separated is first subjected to a detergent, known as SDS (sodium dodecyl sulfate). This detergent denatures the protein. The 3D structure of the protein will not be revealed after separation. Samples move in PAGE gel, only on basis of size.In Native PAGE, the protein being separated is not subjected to any detergent. This means that the protein remains as it is. It is being separated from its native form intact. The 3D structure of the protein can be revealed after separation. Here the samples move on the basis of size and charge.In isoelectric focusing, the proteins are separated on the basis of their isoelectric point. The net charge on the protein can also be determined using this technique. Samples move in the gel on the basis of size, charge and isoelectric point.The difference between Polyacrylamide Gel Electrophoresis (PAGE) and Agarose Gel Electrophoresis (AGE)
Explanation:
Native or non denaturing gel electrophoresis is run in the absence of SDS.
- While in SDS-PAGE the electrophoretic mobility of proteins depends primarily on their molecular mass, in native PAGE the mobility depends on both the protein' s charge and its hydrodynamic size.