P0 is an abundant myelin glycoprotein of peripheral nerves of vertebrates.
Various point mutations of this protein are responsible for hereditary neur
opathies. In this paper we described purification of P0 glycoprotein using
SDS and a metal chelate affinity chromatography. Purified myelin fraction f
rom bovine spinal roots in 0.5% SDS, 0.5 M NaCl, 50 mM Tris-HCl, pH 7.4 is
filtered and applied directly to the Cu2+-immobilized affinity chromatograp
hy column, equilibrated with the same buffer. After eluting a void volume (
or pass through) fraction, P0 protein was eluted by the same buffer but wit
hout salt. To remove contamination from the eluent, further purification is
continued on a Concanavalin-A coupled agarose column. We purify within two
days, 30 mg of P0 protein of apparent molecular weight 27 kDa. The method
can be used to purify recombinant or mutated P0 protein found in severe pat
hologies.