Peroxidase-Like Catalytic Activity of Aqueous- and Immobilized-Mn3+-octabromo-porphyrins on Ion-Exchange Resin Supplied as Mimetic of Horseradish Peroxidase

  • Kitamura Youji
    Department of Pharmaceutical Sciences, Graduate School of Medicine and Dentistry and Pharmaceutical Sciences, Okayama University
  • Mori Katsuya
    Department of Pharmaceutical Sciences, Graduate School of Medicine and Dentistry and Pharmaceutical Sciences, Okayama University
  • Yamamoto Makiko
    Department of Pharmaceutical Chemistry, Graduate School of Natural Science and Technology, Okayama Universi-ty
  • Nozaki Akira
    Department of Pharmaceutical Chemistry, Graduate School of Natural Science and Technology, Okayama Universi-ty
  • Saito Madoka
    Faculty of Pharmaceutical Sciences, Mukogawa Women's University
  • Tsukamoto Ikuko
    Faculty of Medicine, Kagawa University
  • Mifune Masaki
    Department of Pharmaceutical Sciences, Graduate School of Medicine and Dentistry and Pharmaceutical Sciences, Okayama University
  • Saito Yutaka
    Department of Pharmaceutical Sciences, Graduate School of Medicine and Dentistry and Pharmaceutical Sciences, Okayama University

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In order to explore the capability of metal porphyrins as an alternative of horseradish peroxidase (HRP), HRP-like activi-ty of three manganese-porphyrins (Mn-Ps) and three Mn-octabromo-porphyrins (Mn-OBPs) was examined in both aqueous and immobilized states. It was found that Mn3+-octabromotetrakis(1-methyl-pyridinium-4yl)porphine (Mn-OBTMPyP) has an activity of at least 90% of HRP in an aqueous solution. Mn-OBTMPyP exhibited a catalytic activity even in the presence of hydrogen peroxide without suicide reaction. In addition, Mn-OBTMPyP was revealed to function as an alternative to HRP in the quantitative determination of serum uric acid. These results are of great interest because they indicate that metal-octabromo-porphyrins possibly include promising candidates of artificial enzyme capable of substituting for HRP.

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