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应用ＣＭ－ＳｅｐｈａｄｅｘＣ－５０离子交换层析法，从长白山白眉蝮蛇毒中分离出２个具有磷脂酶Ａ２（ＰｈｏｓｐｈｌｉｐａｓｅＡ２，ＰＬＡ２）活性的蛋白质组分。其中之一再经ＤＥＡＥ－ＣｅｌｌｕｌｏｓｅＡ－５２离子交换层析和ＳｅｐｈａｄｅｘＧ－５０凝胶过滤进一步纯化，经两种不同类型的聚丙烯酸胺凝胶电泳鉴定均为单一条带，ＳｅｐｈａｄｅｘＧ－５０凝胶过滤呈单一对称的峰形。
CM-Sephadex C-50 ion exchange chromatography was used to separate two protein fractions with phospholipase A2 (PLA2) activity from Changbai Mountain Bai Mei snake venom. One of them was further purified by DEAE-Cellulose A-52 ion exchange chromatography and Sephadex G-50 gel filtration. The two bands were identified by two different types of polyacrylamide gel electrophoresis. The single phase was used for Sephadex G-50 gel filtration. Symmetrical peak shape.