Alpeeva Inna S, Yu Sakharov Ivan
Chemical Enzymology Department, Faculty of Chemistry, The M.V. Lomonosov Moscow State University, Moscow, 119992, Russia.
Luminescence. 2007 Mar-Apr;22(2):92-6. doi: 10.1002/bio.931.
Anionic sweet potato peroxidase (SPP; Ipomoea batatas) was shown to efficiently catalyse luminol oxidation by hydrogen peroxide, forming a long-term chemiluminescence (CL) signal. Like other anionic plant peroxidases, SPP is able to catalyse this enzymatic reaction efficiently in the absence of any enhancer. Maximum intensity produced in SPP-catalysed oxidation of luminol was detected at pH 7.8-7.9 to be lower than that characteristic of other peroxidases (8.4-8.6). Varying the concentrations of luminol, hydrogen peroxide and Tris buffer in the reaction medium, we determined favourable conditions for SPP catalysis (100 mmol/L Tris-HCl buffer, pH 7.8, containing 5 mmol/L hydrogen peroxide and 8 mmol/L luminol). The SPP detection limit in luminol oxidation was 1.0 x 10(-14) mol/L. High sensitivity in combination with the long-term CL signal and high stability is indicative of good promise for the application of SPP in CL enzyme immunoassay.
阴离子型甘薯过氧化物酶（SPP；来自甘薯）已被证明能有效地催化过氧化氢对鲁米诺的氧化，形成长期的化学发光（CL）信号。与其他阴离子型植物过氧化物酶一样，SPP能够在没有任何增强剂的情况下有效地催化这种酶促反应。在pH 7.8 - 7.9时检测到SPP催化鲁米诺氧化产生的最大强度低于其他过氧化物酶的特征值（8.4 - 8.6）。通过改变反应介质中鲁米诺、过氧化氢和Tris缓冲液的浓度，我们确定了SPP催化的有利条件（100 mmol/L Tris - HCl缓冲液，pH 7.8，含有5 mmol/L过氧化氢和8 mmol/L鲁米诺）。鲁米诺氧化中SPP的检测限为1.0×10⁻¹⁴ mol/L。高灵敏度与长期CL信号和高稳定性相结合，表明SPP在CL酶免疫分析中的应用前景良好。
