A NEW DETERGENT TO PURIFY CNS MYELIN BASIC-PROTEIN ISOFORMS IN LIPID-BOUND FORM

WE have previously shown that CNS myelin basic protein (MBE) can be purified in the lipid-bound, native-like form by using a procedure based on myelin solubilization with detergents at pH above 7, and on the filter-like use of hydroxyapatite to separate non-adsorbed MBP from other myelin proteins. Here, we report on the isolation of MBP in the switterionic detergent 3-(3-cholamidopropyl)dimethylammonio)-1-propane sulfonate (CHAPS), which does not interfere at 280 nm and can be removed by dialysis. This detergent appears to improve MBP purification and to be suitable for florescence and reconstitution studies that can be useful to understand both structure and function of MBP in its natural environment.