摘要
作者报道了从大肠杆菌超表达菌株ＪＣ１１２７２中，制备重组酶ＲｅｃＡ蛋白的研究．利用亚精胺选择性沉淀，单链ＤＮＡ纤维素亲和层析及阳离子换柱ＭｏｎｏＱ进行离子交换层析，从２升超表达细菌培养物中提纯了５５ｍｇ的ＲｅｃＡ蛋白．通过９％ＳＤＳＰＡＧＥ电泳检测结果表明，纯化的ＲｅｃＡ蛋白纯度达９９．５％，具有催化同源ＤＮＡ链交换的能力．
A production of RecA protein from E.coli strain JC11272 was performed.55 mg of RecA was purified from 4 liters culture of E.coli by the spermidine selective precipitation,ssDANcellulose affinity chromatography and Mono Q ion exchange chromatography.The final product was 99.5% pure as judged by 9% SDSPAGE.Theactivity of theis purified protein to catalyze strandexchange between homologous DNA was shown.
出处
《四川大学学报（自然科学版）》
CAS
CSCD
北大核心
1998年第3期477-481,共5页
Journal of Sichuan University(Natural Science Edition)
基金
国家自然科学基金
