Pekelharing J M, Noordeloos P J, Leijnse B
Clin Chim Acta. 1979 Oct 15;98(1-2):61-5. doi: 10.1016/0009-8981(79)90166-9.
The influence of Zn2+ on the inactivation of alkaline phosphatase [orthophosphoric monoester phosphohydrolase (alkaline optimum), EC 3.1 3.1] in serum during preincubation with 2-amino-2-methyl-1-propanol (AMP) buffers was investigated. Addition of Zn2+ to the buffer before preincubation increases the enzyme activity. An optimum Zn2+ concentration different for each lot of AMP buffer can be found, at which the enzyme activities are restored to a level equal to activities measured without preincubation. There is a relation between the inactivating properties of the different AMP buffers and the amount of Zn2+ needed to prevent this inactivation. Since Zn2+ chelating substituted diamines are held responsible for the inactivation by removing Zn2+ from the enzyme, we assume that the addition of Zn2+ to the buffer prevents this removal. As Zn2+ itself is an inhibitor of the enzyme, the addition of both too much or too little Zn2+ results in lower enzyme activities after preincubation with AMP buffer.
研究了锌离子（Zn2+）对血清中碱性磷酸酶[正磷酸单酯磷酸水解酶（最适pH碱性，EC 3.1.3.1）]在与2-氨基-2-甲基-1-丙醇（AMP）缓冲液预孵育期间失活的影响。预孵育前向缓冲液中添加Zn2+可提高酶活性。对于每一批AMP缓冲液，都能找到一个不同的最佳Zn2+浓度，在此浓度下酶活性可恢复到与未进行预孵育时测得的活性相当的水平。不同AMP缓冲液的失活特性与防止这种失活所需的Zn2+量之间存在关联。由于锌离子螯合取代二胺通过从酶中去除Zn2+而导致失活，我们推测向缓冲液中添加Zn2+可防止这种去除。由于Zn2+本身是该酶的抑制剂，因此添加过多或过少的Zn2+都会导致在与AMP缓冲液预孵育后酶活性降低。
