碱性磷酸酶的酶 - 底物复合物和酶 - 磷酸复合物对乙二醇双（2-氨基乙基醚）四乙酸（EGTA）失活作用的抗性。
Resistance to inactivation by EGTA of the enzyme-substrate and enzyme-phosphate complexes of alkaline phosphatase.
作者信息
Pike S J, Duggleby R G
机构信息
Department of Biochemistry, University of Queensland, St. Lucia, Australia.
出版信息
Biochem J. 1987 Jun 15;244(3):781-5. doi: 10.1042/bj2440781.
Bovine intestinal mucosal alkaline phosphatase is inactivated by the chelating agent EGTA. Several concentrations of the enzyme were incubated with EGTA and a range of concentrations of the substrate p-nitrophenyl phosphate to determine the substrate concentration as a function of time. As predicted by a recently developed theory [Duggleby (1986) J. Theor. Biol. 123, 67-80], catalysis ceases before all substrate is exhausted. An analysis of these final substrate concentrations according to the theory revealed that, whereas the free enzyme is unstable, the effect of EGTA is counteracted when either the substrate or product (phosphate) is bound. Comparison of the results with those obtained by direct stability measurements and steady-state kinetic experiments gave a qualitatively and quantitatively consistent body of evidence in support of this interpretation.
牛肠黏膜碱性磷酸酶会被螯合剂乙二醇双四乙酸（EGTA）灭活。将几种浓度的该酶与EGTA以及一系列浓度的底物对硝基苯磷酸酯一起孵育，以确定底物浓度随时间的变化情况。正如最近发展的一种理论所预测的那样[达格利比（1986年），《理论生物学杂志》123卷，67 - 80页]，在所有底物耗尽之前催化作用就停止了。根据该理论对这些最终底物浓度进行分析后发现，虽然游离酶不稳定，但当底物或产物（磷酸盐）结合时，EGTA的作用会被抵消。将这些结果与通过直接稳定性测量和稳态动力学实验获得的结果进行比较，得到了定性和定量上一致的大量证据来支持这一解释。
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