The PO Protein of Chick Sciatic Nerve Myelin: Purification and Partial Characterization

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Abstract
The PO protein of the myelin of chick sciatic nerve was isolated and purified by propanoic acid extraction of peripheral nervous system (PNS) myelin, delipidation, Sepharose CL‐6B chromatography in the presence of sodium dodecyl sulfate (SDS), and preparative SDS‐polyacrylamide gel electro‐phoresis (PAGE). Approximately 15% of the PO protein in the sciatic nerve myelin was recovered in a homogeneous state. The purified protein monomer has an apparent molecular weight of 32.1K as determined by gel electrophoresis. The PO protein undergoes extensive aggregation during exhaustive dialysis and freeze‐drying and yields stable dimers, trimers, and tetramers. The aggregation of the PO protein after freeze‐drying is independent of the presence of a reducing agent (2‐mercaptoethanol) in the solubilizing medium. The PO protein is a glycoprotein. The amino acid composition of the chick PO protein indicates a definite species difference when compared with mammalian PO proteins although the NH2‐terminal isoleucine residue seems to have been retained during evolution.