ABSTRACT
Protein zero (P0) glycoprotein is the major integral membrane protein of the peripheral nervous system myelin in higher vertebrates. Previous findings indicate the formation of tetrameric assemblies from studies on isolated P0. To determine whether in intact myelin the P0 exists as oligomers, we isolated myelin from sciatic nerve of Xenopus laevis and analyzed it using sodium dodecyl sulfate and urea gel electrophoresis. P0 oligomerization was confirmed using Western blotting, which showed monomeric P0 at approximately 30 kDa and oligomeric P0 at approximately 60 kDa and approximately 120 kDa. A variety of denaturing conditions failed to convert any appreciable amount of oligomer to monomer. Instead, the addition of these denaturants further increased the amount of dimer and tetramer while decreasing the amount of monomer. Native gels showed dimeric P0 without the appearance of monomer or tetramer, suggesting that dimeric P0, the most prominent form of the protein, is the most stable and likely occurs in the native myelin membrane array.
