一种受锰离子刺激的小型细菌碱性磷酸酶的分离与特性
Isolation and properties of a small manganese-ion-stimulated bacterial alkaline phosphatase.
作者信息
Fitt P S, Peterkin P I
出版信息
Biochem J. 1976 Jul 1;157(1):161-7. doi: 10.1042/bj1570161.
Abstract
- An alkaline phosphatase was partially purified from extracts of Halobacterium cutirubrum. 2. The enzyme has a mol.wt. of 15 500 and is therefore less than one-quarter of the size of other known bacterial alkaline phosphatases. 3. It is stimulated up to ten-fold by Mn2+, but not by Ca2+ or Mg2+. 4. The activities with and without Mn2+ cannot be separated by gel filtration and have similar restricted substrate specificities. 5. The only substrates for the enzyme that have so far been found are p-nitrophenyl phosphate, 5'-dATP, 5'-dTMP and 5'-dTTP.
摘要
- 从深红嗜盐菌提取物中部分纯化出一种碱性磷酸酶。2. 该酶的分子量为15500，因此小于其他已知细菌碱性磷酸酶大小的四分之一。3. 它受到锰离子的刺激，活性可提高至十倍，但不受钙离子或镁离子的刺激。4. 有锰离子和无锰离子时的活性不能通过凝胶过滤分离，且具有相似的受限底物特异性。5. 迄今为止发现的该酶的唯一底物是对硝基苯磷酸酯、5'-脱氧腺苷三磷酸、5'-脱氧胸苷酸和5'-脱氧胸苷三磷酸。
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