PMID: 6168744Sep 1, 1981Paper

The PO protein of chick sciatic nerve myelin: purification and partial characterization

Journal of Neurochemistry
C Mezei, J A Verpoorte

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 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.

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Citations

Jul 1, 1987·Journal of the Neurological Sciences·P MilnerR A Hughes
Jun 1, 1985·Brain Research·A C Leblanc, C Mezei
Jan 1, 1987·Comparative Biochemistry and Physiology. B, Comparative Biochemistry·A C LeBlanc, C Mezei
Sep 13, 2014·Journal of Neuroscience Research·Jan SedzikMarina Grandis
Jan 1, 1984·Journal of Neurochemistry·D J Nunn, C Mezei
May 1, 1986·Journal of Neurochemistry·Y UchidaK Nomura
Mar 1, 1990·Journal of Neuroscience Research·L H van den BergN Latov

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