p-Nitrophenylphosphorylcholine is a synthetic chromogenic substrate commonly used in colorimetric detection of phospholipase C and related phosphodiesterase activities [1]. Under alkaline or neutral buffer conditions, p-Nitrophenylphosphorylcholine is hydrolyzed by the enzyme to release yellow p-nitrophenol (pNP), which has a characteristic absorption peak near 405nm, facilitating quantitative monitoring of enzyme activity by UV-Vis spectroscopy [2-3].
References:
[1]. Berka R M, Gray G L, Vasil M L. Studies of phospholipase C (heat-labile hemolysin) in Pseudomonas aeruginosa[J]. Infection and Immunity, 1981, 34(3): 1071-1074.
[2]. Martin L M. Facile reduction in the synthesis of phosphorylcholine affinity columns[J]. Tetrahedron letters, 1996, 37(44): 7921-7924.
[3]. Flieger A, Gong S, Faigle M, et al. Critical evaluation of p-nitrophenylphosphorylcholine (p-NPPC) as artificial substrate for the detection of phospholipase C[J]. Enzyme and microbial technology, 2000, 26(5-6): 451-458.
p-Nitrophenylphosphorylcholine是一种合成的显色底物，常用于比色检测磷脂酶C及相关的磷酸二酯酶的活性 [1]。在碱性或中性缓冲条件下，p-Nitrophenylphosphorylcholine被酶水解，释放出黄色的对硝基苯酚（pNP），其在405nm附近具有特征吸收峰，便于通过紫外可见光谱法定量监测酶活性 [2-3]。