Abstract
In acetic acid buffer solution, glucose oxidase (GOD) catalyzed the dissolved oxygen oxidation of glucose to form H2O2. In succession, horseradish peroxidase (HRP) catalyzed the H2O2 oxidizing excess I− to form I3−. The I3− combined with a cationic surfactant (CS) such as tetradecyl dimethyl benzyl ammonium chloride (TDMBA) to produce TDMBA-I3 association particles that exhibited the strongest resonance scattering (RS) peak at 460 nm. The enhanced RS intensity at 460 nm was linear with glucose concentration in the range of 2.0 × 10−8 − 2.0 × 10−6 mol/L, with a detection limit of 8.5 × 10−9 mol/L. The glucose in serum samples were assayed by the enzyme catalytic RS assay and by spectrophotometry. The results of both assays showed a close correlation. This assay has simplicity, sensitivity and good specificity for quantitative determination of glucose.
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Wei, X., Ma, J., Liang, A. et al. A New Enzyme-catalytic Resonance Scattering Assay for Glucose in Serum Using Cationic Surfactant. ANAL. SCI. 25, 887–890 (2009). https://doi.org/10.2116/analsci.25.887
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DOI: https://doi.org/10.2116/analsci.25.887