牙龈卟啉单胞菌甘氨酰脯氨酰氨基肽酶的纯化与鉴定
Purification and characterization of glycylprolyl aminopeptidase from Bacteroides gingivalis.
作者信息
Miyauchi T, Hayakawa M, Abiko Y
出版信息
Oral Microbiol Immunol. 1989 Dec;4(4):222-6. doi: 10.1111/j.1399-302x.1989.tb00256.x.
Abstract
A glycylprocyl aminopeptidase from cell extracts of Bacteriodes gingivalis 381 was purified 1058-fold by hydrophobic adsorbent, HPLC anion exchange, and HPLC gel filtration column chromatography. The final enzyme preparation was homogeneous with a molecular weight of 75,000 daltons by SDS-PAGE, and the isoelectric point was 6.2. The optimum pH of the enzyme was 8.0, and the enzyme activity was inhibited by DFP Ni2+ and Hg2+.
摘要
从牙龈拟杆菌381细胞提取物中获得的一种甘氨酰脯氨酰氨基肽酶，通过疏水吸附剂、高效液相色谱阴离子交换和高效液相色谱凝胶过滤柱色谱法进行纯化，纯化倍数达1058倍。通过SDS-PAGE分析，最终的酶制剂呈均一状态，分子量为75,000道尔顿，等电点为6.2。该酶的最适pH值为8.0，酶活性受到二异丙基氟磷酸、镍离子和汞离子的抑制。
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