Rej R, Bretaudiere J P, Jenny R W, Jackson K Y
Clin Chem. 1981 Aug;27(8):1401-9.
An inactivator of alkaline phosphatase (EC 3.1.3.1) in 2-amino-2-methyl-1-propanol is demonstrated and characterized. This time-dependent inactivation results from chelation of enzyme-bound Zn2+; it is reversed by addition of Zn2+ and, to a lesser extent, other divalent metal ions. Cu2+ is an effective spectral indicator and can be used to determine the presence and quantity of inactivator. Data obtained from enzyme inactivation, Cu2+ absorbance spectra, "high-performance" liquid chromatography, thin-layer chromatography, Fourier-transform infrared spectroscopy, and mass spectroscopy indicate that the inactivator is 5-amino-3-aza-2,2,5-trimethylhexanol. This compound, even in trace amounts (less than 0.05% on a molar basis), shown to inactivate alkaline phosphatase.
在2-氨基-2-甲基-1-丙醇中发现并表征了一种碱性磷酸酶（EC 3.1.3.1）的失活剂。这种时间依赖性失活是由于与酶结合的Zn2+螯合所致；通过添加Zn2+以及在较小程度上添加其他二价金属离子可使其逆转。Cu2+是一种有效的光谱指示剂，可用于确定失活剂的存在和数量。从酶失活、Cu2+吸收光谱、“高效”液相色谱、薄层色谱、傅里叶变换红外光谱和质谱获得的数据表明，失活剂是5-氨基-3-氮杂-2,2,5-三甲基己醇。该化合物即使痕量存在（摩尔比小于0.05%）也能使碱性磷酸酶失活。
