牛乳碱性磷酸酶的催化中心活性及动力学特性
The catalytic-centre activity and kinetic properties of bovine milk alkaline phosphatase.
作者信息
Barman T E, Gutfreund H
出版信息
Biochem J. 1966 Nov;101(2):460-6. doi: 10.1042/bj1010460.
Abstract
- The phosphorylation of milk alkaline phosphatase was studied under various conditions: maximum incorporation occurred at pH5.0 and 50% incorporation at pH6.6-7.0. 2. The phosphorylation was shown to be specific and the results suggest that the active centre of the enzyme is involved in the process. 3. Phosphoryl-enzyme is rapidly hydrolysed at alkaline pH. at pH7.0 the results suggest that a phosphoryl-enzyme could occur as a transient intermediate in the hydrolysis of phosphate esters by the phosphatase. 4. The catalytic-centre activity of the enzyme was found to be 2700sec.(-1) at pH10.0 and 25 degrees with p-nitrophenyl phosphate as substrate.
摘要
- 在不同条件下研究了乳碱性磷酸酶的磷酸化作用：最大掺入量出现在pH5.0时，在pH6.6 - 7.0时掺入量为50%。2. 磷酸化作用具有特异性，结果表明该酶的活性中心参与了这一过程。3. 磷酸化酶在碱性pH下迅速水解。在pH7.0时，结果表明磷酸化酶可能作为磷酸酶水解磷酸酯的瞬时中间体出现。4. 以对硝基苯磷酸酯为底物时，在pH10.0和25℃条件下，该酶的催化中心活性为2700秒⁻¹。
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