葡萄球菌核酸酶去C-末端的肽段52和79的分离纯化  

ISOLATION AND PURIFICATION OF STAPHYLOCOCCAL NUCLEASE PEPTIDE FRAGMENT 52 AND 79

作　　者：耿芳宋[1,2,3] 静国忠[1,2,3] 许小幸[1,2,3] 段建华 王秀丽[1,2,3] 

机构地区：[1]青岛医学院生物化学教研室 [2]中国科学院生物物理研究所 [3]青岛医学院预防医学教研室

出　　处：《青岛医学院学报》1997年第3期195-196,共2页Acta Academiae Medicinae Qingdao Universitatis

基　　金：山东省卫生厅科研基金

摘　　要：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。Objective To establish method for separation and purification of staphylococcal nuclease peptide fragments 52 and 79 with removed carboxy terminal end(SN 52 , SN 79 ). Methods SN 52 and SN 79 were precipitated by cold ethanol, separated and purified through chromatography on sephadex G 50 column and sephacryl S 100 column and identified by sodium dodecyl sulfate polyacrylamide gel electrophoresis(SDS PAGE) and high performance liquid chromatography(HPLC). Results Purified SN52 and SN79 each showed a single band after SDS PAGE and a single peak after HPLC. Conclusion SN 52 and SN 79 of staphylococcal nuclease purified in this study have reached electrophoresis purity and chromatography purity level and can be used for their conformation study.

关 键 词：葡萄球菌 核酸酶 肽片段 提纯 

分 类 号：Q556.03[生物学—生物化学] Q936