| 大肠杆菌AE109青霉素G酰化酶的分离纯化及性质研究 |
| |
| 引用本文： | 张其玖,颜茂恭,陈红,赵武玲. 大肠杆菌AE109青霉素G酰化酶的分离纯化及性质研究[J]. 中国生物化学与分子生物学报, 1990, 6(4): 327-333 |
| |
| 作者姓名： | 张其玖 颜茂恭 陈红 赵武玲 |
| |
| 作者单位： | 中国科学院生物物理研究所，中国科学院生物物理研究所，中国科学院生物物理研究所，北京农业大学生物工程学院 北京 |
| |
| 摘 要： | 由发酵培养液所得大肠杆菌AE109菌体,先经高渗休克处理,继经D-苯甘氨酸-Sepharose 4B和DEAE-纤维素柱层析分离纯化得到青霉素G酰化酶,酶制品在非变性条件下的聚丙烯酰胺凝胶电泳上呈一条区带,而且可以结晶。在SDS变性条件下解离为α和β两个亚基。 酶性质的研究结果表明,由大肠杆菌工程菌AE109菌株所得青霉素G酰化酶与其亲本大肠杆菌AS1.76菌株所得青霉素G酰化酶性质相同。
|
| 关 键 词： | 青霉素G酰化酶 疏水层析 酶的性质 |
| 收稿时间： | 1990-08-20 |
The Purification and Properties of Penicillin G Acylase From E.coli AE109 |
| |
| Zhang,Qi-jiu Yan,Mao-gong Chen,Hong. The Purification and Properties of Penicillin G Acylase From E.coli AE109[J]. Chinese Journal of Biochemistry and Molecular Biology, 1990, 6(4): 327-333 |
| |
| Authors: | Zhang Qi-jiu Yan Mao-gong Chen Hong |
| |
| Affiliation: | (Institute of Biophysics, Academia Sinica, Beijing) Zhao, Wu-ling(Department of Biochemistry, College of Biological Science, Beijing Agricultural University, Beijing |
| |
| Abstract: | Penicillin G acylase has been isolated and purified from E.coli AE109 by treating with high osmotic shock followed by hydrophobic interaction chromatography and DEAE-cellulose chromatography .Electrophoresis analysis shown that the enzyme preparation has a high purity and can be crystallized. The enzyme was dissociaertd into subunit α and β on denaturing SDS-PAGE.Studies on the enzyme properties shown that the penicillin G acylase from E, coli AE109 strain is identical with the enzyme from one of the parent strain E. coli As 1.76. |
| |
| Keywords: | Penicillin G acylase hydrophobia interaction chromatography Properties of the enzyme |
| 本文献已被 CNKI 等数据库收录！ |
| 点击此处可从《中国生物化学与分子生物学报》浏览原始摘要信息 |
|
点击此处可从《中国生物化学与分子生物学报》下载全文 |
