Sugii S, Hirota Y
Department of Serology and Immunology, School of Medical Technology, Kitasato University, Kanagawa, Japan.
J Vet Med Sci. 1993 Oct;55(5):841-3. doi: 10.1292/jvms.55.841.
A Ca(2+)-dependent phosphorylcholine (PC)-binding protein in normal chicken serum was purified by affinity chromatography on p-aminophenyl PC-Sepharose 4B followed by gel filtration on Sephacryl S-300. In gel filtration, the isolated PC-binding protein was eluted in a symmetrical protein peak at the position of approximately 100,000. On sodium dodecyl sulfate-polyacrylamide gel electrophoresis, the protein was resolved into two protein bands of 31,000 and 38,000 under nonreducing conditions and of 40,000 and 46,000 under reducing conditions. These results suggest that chicken serum PC-binding protein may be composed of two different subunits which contain intrachain disulfide bonds.
通过对氨基苯基磷酰胆碱-琼脂糖4B亲和层析，随后在Sephacryl S-300上进行凝胶过滤，纯化了正常鸡血清中一种依赖钙离子的磷酰胆碱（PC）结合蛋白。在凝胶过滤中，分离出的PC结合蛋白在约100,000位置处以对称的蛋白峰被洗脱。在十二烷基硫酸钠-聚丙烯酰胺凝胶电泳中，该蛋白在非还原条件下分解为31,000和38,000的两条蛋白带，在还原条件下分解为40,000和46,000的两条蛋白带。这些结果表明，鸡血清PC结合蛋白可能由两个不同的亚基组成，这两个亚基含有链内二硫键。
