| Project/Area Number |
11794016
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| Research Category |
Grant-in-Aid for University and Society Collaboration
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| Allocation Type | Single-year Grants |
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| Research Field |
General pharmacology
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| Research Institution | KUMAMOTO UNIVERSITY |
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Principal Investigator |
NISHI Katsuhide Kumamoto University, School of Medicine, Professor, 医学部, 教授 (00040220)
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| Co-Investigator(Kenkyū-buntansha) |
UNO Tadayuki Kumamoto University, Faculty of Pharmaceutical Sciences, Professor, 薬学部, 教授 (00183020)
OTAGIRI Masaki Kumamoto University, Faculty of Pharmaceutical Sciences, Professor, 薬学部, 教授 (80120145)
MAEDA Hiroshi Kumamoto University, School of Medicine, Professor, 医学部, 教授 (90004613)
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| Project Period (FY) |
1999 – 2001
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| Project Status |
Completed (Fiscal Year 2001)
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| Budget Amount *help |
¥25,000,000 (Direct Cost: ¥25,000,000)
Fiscal Year 2001: ¥25,000,000 (Direct Cost: ¥25,000,000)
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| Keywords | pyridoxalated hemoglobin polyoxyethylene conjugate / α_1-acid glycoprotein / S-nitrosylation / human serum albumin / recombinant human serum albumin / cytochrome b562 / 酸化アルブミン / Cys残基 / ミオグロビン / 配位子結合性 / α-1酸性糖タンパク / 細隙通過促進作用 / 微細循環改善作用 / 白血球走化性抑制作用 / 炎症 / 変異アルブミン / ミオグロビン変異体 / シトクロムb562変異体 / 人口酸素運搬体 / ポリオキシエチレン・重合ヘモグロビン(PHP) / αー1酸性糖タンパク / 血流阻害抑制作用 / 組換え型HSA / 血漿由来HSA |
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| Research Abstract |
Nishi et al. found the inhibitory effects of pyridoxalated hemoglobin polyoxyethylene conjugate (PHP) on the intestinal peristaltic movement, the facilitatory effect of α_1-acid glycoprotein (α_1-AGP) on the passage of red blood cells through filters with micropores, and the vasodilator action of α_1-AGP in aorta.
Maeda et al. found that S-nitrosylation of α_1-protease inhibitor (α_1-PI) occurring under physiological conditions should diverse in the biological functions contributing to cytoprotective effects of α_1-PI, and suggested that S-nitrosylated α_1-AGP would have the multiple biological functions.
Otagiri et al. purified recombinant human serum albumin (rHSA), secreted by a Pichia pastoris expression system, and showed very similar structural characteristics, stability and ligand-binding properties of the rHSA as HSA isolated from sera.
Uno et al. analyzed the amino acid residues surrounding the cofactor in the structures of a four-helix bundle heme protein, cytochrome b562 from E. coli, and developed a strategy for designing an exogenous ligand binding pocket into this protein.
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