The PO Protein of Chick Sciatic Nerve Myelin: Purification and Partial Characterization
- 1 September 1982
- journal article
- research article
- Published by Wiley in Journal of Neurochemistry
- Vol. 37 (3), 550-557
- https://doi.org/10.1111/j.1471-4159.1982.tb12522.x
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 electrophoresis (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 MW 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.Keywords
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