超氧化物歧化酶的某些性质及胰酶酶解的研究

超氧化物歧化酶的某些性质及胰酶酶解的研究 CHARACTERIZATION AND TRYPSIN DIGESTION OF SUPEROXIDE DISMUTASE 刘利东 Liu Lidong Zou Guolin Zhu Rufan 1 first-author 邹国林 1 朱汝璠 1 武汉大学生物系 武汉大学生物系 Department of Biology,Wuhan University Department of Biology,Wuhan University 按本室制备方法,从1000ml 鸡红细胞中得30mg 纯超氧化物歧化酶（Cu·Zn-SOD）,比活力为16600u/mg,经检测所得酶是均一的。用 DNS 法测得该酶 N-末端氨基酸为丙氨酸。在紫外和可见光区的特征吸收峰分别在260nm 和680nm,用 Sephadex G-100凝胶过滤法测得分子量为33800道尔顿,经 SDS—PAGE 测得其亚基分子量为16500道尔顿,由大约154个氨基酸残基组成,不含色氨酸。此外,对猪血 Cu·Zn-SOD 进行了胰酶酶解,得具 Cu·Zn-SOD 活性分子片段。 Copper/Zinc superoxide dismutase from chicken erythrocytes has been isolated and purified by an improving method.From 1000ml chicken erythroc- ytes,30mg Cu.Zn-SOD with specific activity 16600 units per mg protein was obtained.The purified enzyme is found to be homogeneous by the analysis of N tarminal amino acid,disc-PAGE,SDS-PAGE.The chicken erythrocytes SOD exhibits an absorption maximum at 260nm and another at 680nm.The enzyme subunit molecular weight and the molecular weight are 16,500 and 33,800 d.t.respectively.The subunit consists of approximate 154 amino acid residues,in which tryptophan residue is absent.The N terminal amino acid is Ala as assayed by dansyl chloride. At pH8.0,the porcine SOD was digested with trypsin at 37℃ for several days.The result shows that from this reaction,a series of tryptic peptide which had the activity of SOD were obtained. 超氧化物歧化酶 性质 胰酶酶解 鸡红细胞 猪红细胞 superoxide dismutase characterization trypsin digestion chicken erythrocytes porcine erythrocytes 1991-01-01 2021-04-01 1