Molecular mechanism of crystallization enzyme
| Project/Area Number |
24770124
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| Research Category |
Grant-in-Aid for Young Scientists (B)
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| Allocation Type | Multi-year Fund |
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| Research Field |
Functional biochemistry
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| Research Institution | Osaka University |
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Principal Investigator |
ISHIKAWA Haruto 大阪大学, 理学(系)研究科(研究院), 講師 (40551338)
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| Project Period (FY) |
2012-04-01 – 2014-03-31
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| Project Status |
Completed (Fiscal Year 2013)
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| Budget Amount *help |
¥4,680,000 (Direct Cost: ¥3,600,000、Indirect Cost: ¥1,080,000)
Fiscal Year 2013: ¥2,340,000 (Direct Cost: ¥1,800,000、Indirect Cost: ¥540,000)
Fiscal Year 2012: ¥2,340,000 (Direct Cost: ¥1,800,000、Indirect Cost: ¥540,000)
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| Keywords | 金属タンパク質 / ヘム / 酵素 / マラリア |
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| Research Abstract |
Heme detoxification protein (HDP), potent in converting heme into an insoluble crystalline form called hemozoin (Hz), was found in the malaria parasite. We succeeded in the identification of the critical amino acid residues for the Hz formation by using the site-directed mutagenesis, ESR, and resonance Raman measurements. We also investigated that the active site residues in alpha - glucosidase (AGLU) in a blood-sucking bug. Spectroscopic characterization of the recombinant AGLU revealed that a histidine residue exists in the active site.
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Report
(3 results)
Research Products
(24 results)
