| Budget Amount *help |
¥3,720,000 (Direct Cost: ¥3,300,000、Indirect Cost: ¥420,000)
Fiscal Year 2010: ¥650,000 (Direct Cost: ¥500,000、Indirect Cost: ¥150,000)
Fiscal Year 2009: ¥650,000 (Direct Cost: ¥500,000、Indirect Cost: ¥150,000)
Fiscal Year 2008: ¥520,000 (Direct Cost: ¥400,000、Indirect Cost: ¥120,000)
Fiscal Year 2007: ¥1,900,000 (Direct Cost: ¥1,900,000)
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| Research Abstract |
Many people believe that the trigger of the quaternary structural transition of hemoglobin (Hb) is the displacement of the proximal His, which is the only amino acid binding directly to the heme iron (trigger model). I inspected the model by synthesizing the recombinant Hbs, in which the proximal His is replaced with Gly in the α or β subunit, and then analyzing the conformational change and the oxygen carrying mechanism of these Hbs. I have suggested that the shift of the proximal His in the α subunit is the trigger of the structural transition of Hb, whereas one of the β subunit is not the trigger because the conformational change is partially observed in the recombinant Hb without the β proximal His.
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