Techniques for Measuring Carbonic Anhydrase Activity in Vitro
Techniques for Measuring Carbonic Anhydrase Activity in Vitro
复制标题
体外测量碳酸酐酶活性的技术
DOI：
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发表时间：
1991
期刊：
影响因子：
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通讯作者：
R. Henry
中科院分区：
文献类型：
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作者：
R. Henry
本文报道了碳酸酐酶（CA）（EC 4.2.1.1.）催化二氧化碳和水的可逆水合-脱水，H+离子在酶的活性位点和周围的缓冲液之间转移。3，16，17这导致反应向平衡进行时pH值的变化。随着快速响应pH和参比电极与灵敏pH计耦合的出现，可以准确测量H+离子浓度的这些变化。该测量可以直接或间接进行，形成了用于测定CA活性的电测量方法所依据的基本原理。
The isozymes of carbonic anhydrase (CA) (EC 4.2.1.1.) catalyze the reversible hydration—dehydration of carbon dioxide and water, with H+ ions being transferred between the active site of the enzyme and a surrounding buffer.3,16,17 This results in a change in pH as the reaction proceeds toward equilibrium. With the advent of rapid-responding pH and reference electrodes coupled to sensitive pH meters, these changes in H+ ion concentration could be accurately measured. That measurement, which can be performed either directly or indirectly, forms the underlying principle upon which the electrometric methods for the assay of CA activity are built.