| Project/Area Number |
01490017
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| Research Category |
Grant-in-Aid for General Scientific Research (B)
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| Allocation Type | Single-year Grants |
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| Research Field |
広領域
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| Research Institution | Hiroshima University |
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Principal Investigator |
SATO Kiyotaka Hiroshima University, Faculty of Applied Biological Science, Professor, 生物生産学部, 教授 (80034479)
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| Co-Investigator(Kenkyū-buntansha) |
ESAKA M. Hiroshima University, Faculty of Applied Biological Science, Assoc. Professor, 生物生産学部, 助教授 (70151975)
HORI K. Hiroshima University, Faculty of Applied Biological Science, Assoc. Professor, 生物生産学部, 助教授 (50116662)
NAGMATSU Y. Hiroshima University, Faculty of Applied Biological Science, Assoc. Professor, 生物生産学部, 助教授 (30144893)
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| Project Period (FY) |
1989 – 1991
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| Project Status |
Completed (Fiscal Year 1991)
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| Budget Amount *help |
¥5,800,000 (Direct Cost: ¥5,800,000)
Fiscal Year 1991: ¥600,000 (Direct Cost: ¥600,000)
Fiscal Year 1990: ¥800,000 (Direct Cost: ¥800,000)
Fiscal Year 1989: ¥4,400,000 (Direct Cost: ¥4,400,000)
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| Keywords | Protein crystallization / Lattice defect / Toxic protein / Algae lectin / Secreted protein / タンパク質晶化 / 結晶欠陥 / 毒性タンパク質 / たんぱく質 / 結晶化 / 植物細胞分泌タンパク質 / 卵白リゾチ-ム / 光散乱トモグラフ法 / 有用たんぱく質 / たんぱく質の結晶化 / lepidopteran toxin / Ado Hcy hydrolase / メチル基転移反応酵素 |
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| Research Abstract |
Crystallization processes of a model substance : hen-egg white lysozyme were analyzed with laser scattering tomography, etching technique, heterogeneous crystallization and optical microscopy. The crystallization kinetics of an orthorhombic modification was linearly dependent in a logarithmic manner on the concentration of precipitants. The effects of polymorphs were observed in the crystallization kinetics. Lattice defects in lysozyme crystals were examined with laser scattering tomography and etching technique. The defects of point type were concentratedly distributed closer to the growing surfaces and growth sectors were observed. Heterogeneous crystallization on glass and polymer substrates was tried to selectively grow single crystals.
Crystallization of three proteins was newly challenged : toxin protein yielded in bacteria, vegetable cell-producing protein and lectin produced from algae. Pure samples of about 1 0 mg yield of each substance was obtained from raw materials, and subjected to crystallization using vapor diffusion method. However, amorphous solids have so far been obtained. Further trials are needed for these substances.
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