Proteins that have a greater hydrophobic content, for instance many membrane proteins, and those that interact with surfactants in their native environment, are intrinsically harder to treat accurately using this method, due to the greater variability in the ratio of bound SDS. Procedurally, using both Native and SDS Page together, can be used to purify and to separate the various subunits of the protein. Native Page keeps the oligomeric form intact and will show a band on the gel that is representative of the level of activity. Whereas, SDS Page will denature and separate the oligomeric form into its monomers and will show bands that is representative to their molecular weights. These bands can be used to access the purity of and identify the protein.
| This user is a student editor in Wikipedia:Wiki_Ed/Hunter_College/Chemistry_378_(Spring_2017). Student assignments should always be carried out using a course page set up by the instructor. It is usually best to develop assignments in your sandbox. After evaluation, the additions may go on to become a Wikipedia article or be published in an existing article. |