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Title: Isoelectric focusing of membrane proteins: high resolution separation of myelin proteins. Author: Persson H, Corneliuson O. Journal: Electrophoresis; 1989 Nov; 10(11):747-51. PubMed ID: 2515057. Abstract: A mixture of the nonionic detergent Triton X-100, the zwitterionic detergent 3-[(cholamidopropyl)dimethylammonio]-1-propanesulphonate (CHAPS), 9M urea and carrier ampholytes was found comparable to media containing sodium dodecyl sulfate in the capacity for solubilization of myelin proteins, including the highly hydrophobic proteolipid protein. The solubilized sample was incorporated into the polymerization mixture before moulding an ultrathin gel, with heat convection characteristics allowing a high wattage to be applied, thus allowing fast separation with high resolving power. Since the most basic protein in myelin focuses at a pH greater than 10, fast separation is essential in order to minimize decay of the cathodic end of the pH gradient.[Abstract] [Full Text] [Related] [New Search]