A chemiluminescence-based catalase assay using H2O2-sensitive CdTe quantum dots

被引:14
作者
Ghavamipour, Fahimeh [1 ]
Sajedi, Reza H. [1 ]
Khajeh, Khosro [1 ]
机构
[1] Tarbiat Modares Univ, Fac Biol Sci, Dept Biochem, Tehran 14115154, Iran
关键词
Michaelis constant; Substrate saturation; Hydrogen-peroxide: Hydrogen-peroxide oxidoreductase; H2O2; Catalase; Colloidal semiconductor nanocrystals; Chemiluminescence assay; CdTe quantum dots; BOVINE LIVER CATALASE; HYDROGEN-PEROXIDE; ENHANCED CHEMILUMINESCENCE; NANOCRYSTALS; IMMOBILIZATION; FLUORESCENCE; OXIDASE; GLUCOSE;
D O I
10.1007/s00604-018-2912-5
中图分类号
O65 [分析化学];
学科分类号
070302 ; 081704 ;
摘要
A method is described for the chemiluminescence based determination of the activity of catalase (CAT) using H2O2-sensitive CdTe quantum dots (QDs). It is based on the finding that the chemiluminescence (CL) of the CdTe/H2O2 system is reduced due to the consumption of H2O2 by the catalytic action of CAT. The Michaelis constant is calculated to be 519 +/- 27 mM, showing the potential of the method to accurately measure the K-m compared to the standard method. The method does not require QDs to be conjugated to biological/organic molecules and therefore is considered to be a rapid and convenient method for determination of CAT in real samples. At an incubation time of 2 s, the LOD was calculated to be 4.5 unit/mL, with a linear range from 6 to 400 unit/mL. The assay is sensitive, simple, and suitable for practical applications.
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页数:8
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共 35 条
  • [1] Development of novel flexible sugar ester vesicles as carrier systems for the antioxidant enzyme catalase for wound healing applications
    Abdel-Mageed, Heidi M.
    El-Laithy, Hanan M.
    Mahran, Laila G.
    Fahmy, Afaf S.
    Maeder, Karsten
    Mohamed, Saleh A.
    [J]. PROCESS BIOCHEMISTRY, 2012, 47 (07) : 1155 - 1162
  • [2] Immobilization and characterization of bovine liver catalase on eggshell
    Alptekin, Ozlem
    Tukel, S. Seyhan
    Yildirim, Deniz
    [J]. JOURNAL OF THE SERBIAN CHEMICAL SOCIETY, 2008, 73 (06) : 609 - 618
  • [3] Immobilization of catalase onto Eupergit C and its characterization
    Alptekin, Ozlem
    Tukel, S. Seyhan
    Yildirim, Deniz
    Alagoz, Dilek
    [J]. JOURNAL OF MOLECULAR CATALYSIS B-ENZYMATIC, 2010, 64 (3-4) : 177 - 183
  • [4] BEERS RF, 1952, J BIOL CHEM, V195, P133
  • [5] CATALASE ACTIVITY
    BONNICHSEN, RK
    CHANCE, B
    THEORELL, H
    [J]. ACTA CHEMICA SCANDINAVICA, 1947, 1 (08): : 685 - 709
  • [6] Çetinus SA, 2000, ENZYME MICROB TECH, V26, P497, DOI 10.1016/S0141-0229(99)00189-1
  • [7] THE MECHANISM OF CATALASE ACTION .1. STEADY-STATE ANALYSIS
    CHANCE, B
    GREENSTEIN, DS
    ROUGHTON, FJW
    [J]. ARCHIVES OF BIOCHEMISTRY AND BIOPHYSICS, 1952, 37 (02) : 301 - 321
  • [8] Diversity of structures and properties among catalases
    Chelikani, P
    Fita, I
    Loewen, PC
    [J]. CELLULAR AND MOLECULAR LIFE SCIENCES, 2004, 61 (02) : 192 - 208
  • [9] Quantum dots-enhanced chemiluminescence: Mechanism and application
    Chen, Hui
    Lin, Ling
    Li, Haifang
    Lin, Jin-Ming
    [J]. COORDINATION CHEMISTRY REVIEWS, 2014, 263 : 86 - 100
  • [10] Plasmonic luminescent core-shell nanocomposites-enhanced chemiluminescence arising from the decomposition of peroxomonosulfite
    Chen, Hui
    Xue, Wei
    Lu, Chao
    Li, Hai-fang
    Zheng, Yongzan
    Lin, Jin-Ming
    [J]. SPECTROCHIMICA ACTA PART A-MOLECULAR AND BIOMOLECULAR SPECTROSCOPY, 2013, 116 : 355 - 360