| Project/Area Number |
05670116
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| Research Category |
Grant-in-Aid for General Scientific Research (C)
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| Allocation Type | Single-year Grants |
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| Research Field |
General medical chemistry
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| Research Institution | Kanazawa University |
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Principal Investigator |
NAGAI Masako Kanazawa University, School of Allied Medical Professions, Professor, 医療技術短期大学, 教授 (60019578)
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| Co-Investigator(Kenkyū-buntansha) |
中島 広志 金沢大学, 医療技術短期大学部, 助教授 (20020026)
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| Project Period (FY) |
1993 – 1994
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| Project Status |
Completed (Fiscal Year 1994)
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| Budget Amount *help |
¥2,100,000 (Direct Cost: ¥2,100,000)
Fiscal Year 1994: ¥600,000 (Direct Cost: ¥600,000)
Fiscal Year 1993: ¥1,500,000 (Direct Cost: ¥1,500,000)
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| Keywords | Hemoglobin / Ultraviolet Resonance Raman / Circular Dichroism / Protein Structure / Function of Hemoglobin / Aromatic Amino Acids / 赤外分光 / 円二色性 / 異常血色素 / 共鳴ラマン |
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| Research Abstract |
X-ray crystallographic studies have shown that the deoxy and liganded forms of hemoglobin (Hb) poseesee two distinct quaternary structures named T-and R-states, respectively. Cooperative oxygenation to Hb has been explained in terms of a reversible transition between the two quaternary structures upon partial ligation to the four hemes. Environmental changes of tyrosine (Tyr) and tryptophan (Trp) residues of Hb upon its T-to-R transition of quaternary structure was ivestigated with ultraviolet resonance Raman (UVRR) spectroscopy and circular dichroism (CD) . To characterize the spectral change of Trp beta37 at alpha_1beta_2 interface due to the quaternary structure transition, the UVRR spectra of Hb A were compared with the corresponding spectra of Hb Hirose in which Trp beta37 is replaced by serine (Ser) . Difference spectrum between deoxyHb A and deoxyHb Hirose gave rise to only Trp RR bands, which were reasonably ascribed to Trp beta37 in deoxyHb A.Comparison of the Hb A-Hb Hirose difference spectra in the oxy and deoxy states revealed that the oxygenation-induced changes of Trp RR bands arose mostly from Trp beta37 and the remaining minor part from Trp beta15, demonstrating that Trp beta37 plays a pivotal role in the quaternary structural change in Hb A.
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