【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。更多还原

【Abstract】 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.更多还原