Mezei C, Verpoorte J A
J Neurochem. 1981 Sep;37(3):550-7. doi: 10.1111/j.1471-4159.1982.tb12522.x.
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.
通过对周围神经系统（PNS）髓磷脂进行丙酸提取、脱脂、在十二烷基硫酸钠（SDS）存在下进行琼脂糖CL - 6B色谱分析以及制备性SDS - 聚丙烯酰胺凝胶电泳（PAGE），分离并纯化了鸡坐骨神经髓磷脂的PO蛋白。坐骨神经髓磷脂中约15%的PO蛋白以均一状态回收。经凝胶电泳测定，纯化的蛋白单体表观分子量为32.1K。PO蛋白在彻底透析和冷冻干燥过程中会发生广泛聚集，形成稳定的二聚体、三聚体和四聚体。冷冻干燥后PO蛋白的聚集与溶解介质中还原剂（2 - 巯基乙醇）的存在无关。PO蛋白是一种糖蛋白。与哺乳动物的PO蛋白相比，鸡PO蛋白的氨基酸组成显示出明确的物种差异，尽管在进化过程中似乎保留了氨基末端的异亮氨酸残基。
