苏云金杆菌超氧化物歧化酶的纯化和性质研究  

PURIFICATION AND CHARACTERIZATION OF SUPEROXIDE DISMUTASE FROM BACILLUS THURINGIENSIS STRAIN

作　　者：蔡全信[1] 刘娥英[1] 张用梅[1] 袁志明[1] 

机构地区：[1]中国科学院武汉病毒研究所,武汉430071

出　　处：《微生物学通报》1999年第2期110-112,共3页Microbiology China

基　　金：中国科学院区系分类特别支持项目

摘　　要：苏云金杆菌（Ｂａｃｉｌｌｕｓ　ｔｈｕｒｉｎｇｉｅｎｓｉｓ）９１６５超氧化物歧化酶（ＳＯＤ），经硫酸铵分级沉淀、ＳｅｐｈａｄｅｘＦ－１００凝胶过滤及非变性凝胶电泳（ＰＡＧＥ）三步纯化，纯酶比活力为４３８８ｕ／ｍｇ，属Ｍｎ－ＳＯＤ，分子量为４７．９ｋｕ，由二个亚基组成，含１９种氨基酸。Superoxide dismutase from Bacillus thuringiensis 9165 was purified ty a combination of ammonium sulfate fractionation , Sephadex G-100 gel filtration and nondenaturing polyacrylamide gel electiophoresis. The purified enzyme was a highly homogeneous protein with the specific activity of 438.8u/mg. The results of studyshowed that the enzyme was a kind of Mn-SOD composed of two equally sized subunits, with a molecularweight of 47.9ku and it contained nineteen sorts of amino acids.

关 键 词：超氧化物歧化酶 苏云金杆菌 纯化和性质 

分 类 号：Q936[生物学—微生物学] Q939.124