钙亲和层析分离纯化光系统Ⅱ中的钙结合蛋白（Ⅰ）

ISOLATION AND PURIFICATION OF A CALCIUM-BINDING PROTEIN FROM PHOTOSYSTEM Ⅱ THROUGH CALCIUM-CHELATING AFFINITY CHROMATOGRAPHY(Ⅰ)

Ｓｅｐｈａｒｏｓｅ６Ｂ经环氧氯丙烷活化后，与亚氨基二乙酸钠偶联。用钙离子作配体从光系统Ⅱ中分离纯化得到一种钙结合蛋白，在ＳＤＳ－聚丙烯酰胺凝胶上此蛋白呈现单一电泳谱带，分子量约为３０ｋＤａ。根据Ａｒｎｏｎ和Ｂｒａｄｆｏｒｄ方法测定的结果表明该蛋白质是叶绿素ａ／ｂ结合蛋白，每分子蛋白约结合有５分子叶绿素ａ，２分子叶绿素ｂ和一定数量的胡萝卜素分子。

A Calcium-binding protein was purified from photosystem Ⅱ using calcium-chelatingSepharose 6B affinity chromatography,which was activated through 1-2,3-epoxypropane andlinked with disodium salt of iminodiacetic acid.SDS-polyacrylamide gel electrophoresis indicatedthat it was a single band with molecular mass of approximately 30 kDa。Our results reveal that itis a chlorophyll a/b binding protein which binds about five chlorophyll a molecules,two chloro-phyll b molecules and a certain amount of carotenoids.