Journal of Guangxi Normal University(Natural Science Edition) ›› 2012, Vol. 30 ›› Issue (2): 99-105.

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Resonance Scattering Spectral Assay for Alkaline Phosphatase Using BCIP as Substrate

LIANG Ai-hui, LIU Gao-san, JIANG Zhi-liang   

  1. Key Laboratory of Ecology of Rare and Endangered Species and Environmental Protection,Ministry of Education, School of Environment and Resource,Guangxi Normal University,Guilin Guangxi 541004,China
  • Received:2012-04-16 Online:2012-06-20 Published:2018-12-03

Abstract: In pH 8.0 Tris-HCl buffer solutions and in the presence of 32 mg/L PEG20000,using EDTANa2 as terminated agent to stop the enzymatic reaction,alkaline phosphatase (ALP) catalyzed the hydrolysis of 5-bromo-4-Chloro-3-indolylphosphat (BCIP) substrate to form blue BCIP dimer particles,which exhibited a strongresonance scattering (RS) peak at 710 nm.In the selected conditions,with theALP activity increased,the RS intensity (ΔI) linearly increased.ALP activitylinear range was 0.078～1.25 U/L,with a regression equation of ΔI=512.6C+17.8,and a detection limit of 9.6×10-3 U/L.

Key words: 5-bromo-4-chloro-3-indolyl phosphate, alkaline phosphatase, resonance scattering spectroscopy

CLC Number: 

  • O657.3
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