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①目的建立金黄色葡萄球菌核酸酶（ＳＮａｓｅ）去Ｃ－末端的肽段５２（ＳＮ５２）和７９（ＳＮ７９）的提纯方法，并鉴定其纯度。②方法应用低温乙醇沉淀，ＳｅｐｈａｄｅｘＧ－５０和ＳｅｐｈａｃｒｙｌＳ－１００柱层析分离纯化；十二烷基硫酸钠－聚丙烯酰胺凝胶电泳（ＳＤＳ－ＰＡＧＥ）和高效液相层析（ＨＰＬＣ）鉴定其纯度。③结果纯化的ＳＮ５２和ＳＮ７９经ＳＤＳ－ＰＡＧＥ鉴定均为单一区带；ＨＰＬＣ鉴定均为一个峰。④结论纯化的ＳＮ５２和ＳＮ７９已达电泳纯和层析纯，可用于其构象的比较研究。
①Purpose To establish a method to purify the C-terminal peptides 52 (SN52) and 79 (SN79) of S. aureus nuclease (SNase) and identify its purity. ② The method was separated and purified by column chromatography on Sephadex G-50 and Sephacryl S-100 using low temperature ethanol precipitation. Purity was identified by sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) and high performance liquid chromatography (HPLC) . ③ Results The purified SN52 and SN79 were all single bands by SDS-PAGE. HPLC identification showed a single peak. ④ Conclusion Purified SN52 and SN79 have reached electrophoretic purity and chromatographic purity, can be used for the comparison of their conformation.