Sugii S, Hirota Y
Department of Serology and Immunology, School of Medical Technology, Kitasato University, Kanagawa, Japan.
J Vet Med Sci. 1994 Feb;56(1):143-5. doi: 10.1292/jvms.56.143.
A Ca(2+)-dependent agarose-binding protein was purified from chicken serum by affinity chromatography on SeaKem agarose gels followed by gel filtration on Sephacryl S-300. Purified protein was eluted in a symmetrical peak at the position of molecular weight of 146,000. In sodium dodecyl sulfate-polyacrylamide gel electrophoresis, it was resolved into a single protein band with a molecular weight of 39,000 under nonreducing and of 41,000 under reducing conditions. Thus, the agarose-binding protein is suggested to be composed of noncovalently-associated identical subunits which contain intrachain disulfide bonds.
通过在SeaKem琼脂糖凝胶上进行亲和层析，随后在Sephacryl S - 300上进行凝胶过滤，从鸡血清中纯化出一种钙依赖性琼脂糖结合蛋白。纯化后的蛋白在分子量为146,000的位置以对称峰洗脱。在十二烷基硫酸钠 - 聚丙烯酰胺凝胶电泳中，在非还原条件下它被解析为一条分子量为39,000的单一蛋白带，在还原条件下为41,000。因此，推测该琼脂糖结合蛋白由含有链内二硫键的非共价结合的相同亚基组成。
