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白及（Ｂｌｅｉｌｌａｓｔｒｉａｔａ（Ｔｈｕｎｂ．）Ｒｅｉｃｈｂ．ｆ．）的ＳＯＤ同工酶只有一条较宽的谱带，确认为Ｃｕ·Ｚｎ－ＳＯＤ。其块茎ＳＯＤ总活性和比活性都高，且含有丰富的白及胶；经丙酮分级沉淀，ＳｅｐｈａｄｅｘＧ１００凝胶过滤和ＤＥＡＥ－纤维素柱层析分离纯化，获得对ＣＮ￣－敏感的淡兰色Ｃｕ·ＺｎＳｏＤ粉末。在凝胶电泳染色图谱上，纯化后的酶与粗酶液的ＳＯＤ区带相对应，且其酶活性染色带与蛋白染色带位置对应，表明已纯化到均一程度。该酶分子量约３３ＫＤ，亚基分子量约为１６．４ＫＤ；紫外光区的吸收峰在２６４．６ｎｍ，等电聚焦电泳呈现一条蛋白区带，ｐＨ值在４．３５左右；该酶在ｐＨ６．０～１０．０，温度在５０℃范围内具稳定性。纯化后的酶为４５６３．２ｕ／ｍｇ·蛋白，纯化了５１倍，活力回收为２２．３％。上述酶没有过氧化氢酶活性。提取过程中还得到高质量的副产品白及胶。
The SOD isozyme of Bleillastriata (Thunb.) Reichb.f. Has only one broad band, which is confirmed as Cu · Zn-SOD. The tuber SOD total activity and specific activity are high, and is rich in white and gum; acetone precipitation, Sephadex G100 gel filtration and DEAE-cellulose column chromatography to obtain CN ~ -sensitive light blue Cu ZnSoD powder. On the gel electrophoresis, the purified enzyme corresponded to the SOD band of the crude enzyme solution, and its enzymatic activity band corresponded with that of the protein band, indicating that it had been purified to a uniform extent. The molecular weight of the enzyme is about 33KD and the molecular weight of the subunit is about 16.4KD. The UV absorption peak is at 264.6nm. Isoelectric focusing shows a protein band with a pH value of about 4.35. ~ 10.0, temperature stability in the range of 50 ℃. The purified enzyme was 4563.2u / mg · protein, purified 51 times, and the viability recovered was 22.3%. The above enzyme has no catalase activity. The extraction process also gets high quality by-products white and gum.