Recombinant Human Serum Albumin Containing 3 Copies of Domain Ⅰ, Has Significant in Vitro Antioxidative Capacity Compared to the Wild-Type

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  • Matsushita Sadaharu
    Department of Biopharmaceutics, Graduate School of Pharmaceutical Sciences, Kumamoto University
  • Nishi Koji
    Department of Clinical Medicine, Yokohama University of Pharmacy
  • Iwao Yasunori
    Pharmaceutical Engineering Laboratory, School of Pharmaceutical Sciences, University of Shizuoka
  • Ishima Yu
    Department of Pharmacokinetics and Biopharmaceutics, Institute of Biomedical Sciences, Tokushima University
  • Watanabe Hiroshi
    Department of Biopharmaceutics, Graduate School of Pharmaceutical Sciences, Kumamoto University
  • Taguchi Kazuaki
    Faculty of Pharmaceutical Sciences, Sojo University
  • Yamasaki Keishi
    Faculty of Pharmaceutical Sciences, Sojo University DDS Research Institute, Sojo University
  • Maruyama Toru
    Department of Biopharmaceutics, Graduate School of Pharmaceutical Sciences, Kumamoto University
  • Otagiri Masaki
    Faculty of Pharmaceutical Sciences, Sojo University DDS Research Institute, Sojo University

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  • Recombinant Human Serum Albumin Containing 3 Copies of Domain I, Has Significant <i>in Vitro</i> Antioxidative Capacity Compared to the Wild-Type

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<p>Human serum albumin (HSA), the most abundant protein in serum, functions as carrier of drugs and contributes to maintaining serum colloid osmotic pressure. We report herein on the preparation of a genetic recombinant HSA, in which domains II and III were changed to domain I (triple domain I; TDI). Sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) results indicated that the purity of the TDI was equivalent to that of the wild type (WT). Both far- and near-UV circular dichroism (CD) spectra of the TDI showed that its structural characteristics were similar to the WT. Ligand binding capacity was examined by an ultrafiltration method using 3-carboxy-4-methyl-5-propyl-2-furanpropanoic acid (CMPF) and ketoprofen as markers for site I and site II, respectively. The binding capacity of TDI for both ligands was lower than that for the wild type. TDI significantly suppressed the oxidation of dihydrorhodamine 123 (DRD) by H2O2 compared to the WT. Our current results suggest that TDI has great potential for further development as HSA a product having antioxidative functions.</p>

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