WE have previously shown that CNS myelin basic protein (MBE) can be pu
rified in the lipid-bound, native-like form by using a procedure based
on myelin solubilization with detergents at pH above 7, and on the fi
lter-like use of hydroxyapatite to separate non-adsorbed MBP from othe
r myelin proteins. Here, we report on the isolation of MBP in the swit
terionic detergent 3-(3-cholamidopropyl)dimethylammonio)-1-propane sul
fonate (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 us
eful to understand both structure and function of MBP in its natural e
nvironment.