| Project/Area Number |
06672303
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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 |
Laboratory medicine
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| Research Institution | Kitasato University School of Allied Health Sciences |
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Principal Investigator |
OGAWA Zensuke Kitasato University, School of Allied Health Sciences, Department of Clinical Chemistry, Lecturer, 医療衛生学部, 講師 (50152385)
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| Co-Investigator(Kenkyū-buntansha) |
ITOH Hajime Kitasato University, School of Health Sciences, Department of Clinical Chemistry, 医療衛生学部, 教授 (10104564)
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| Project Period (FY) |
1994 – 1995
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| Project Status |
Completed (Fiscal Year 1995)
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| Budget Amount *help |
¥2,200,000 (Direct Cost: ¥2,200,000)
Fiscal Year 1995: ¥900,000 (Direct Cost: ¥900,000)
Fiscal Year 1994: ¥1,300,000 (Direct Cost: ¥1,300,000)
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| Keywords | reaction mechanism / amylase |
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| Research Abstract |
Recently, structure and reaction mechanism of amylase was known by the X-ray analysis and DNA analysis. Many researcher reported that histidine, aspartic acid, glutamic acid and lysine residue of catalytic center playd an important role for the hydrolysis reaction.
We thought the most important role was the recognition of substrate by histidine residue (His). Then, we found out that His modified amylase by diethylpyrocarbonate lost the catalytic activity and this lost activity was recover by the addition of NaN_3. We could suppose the reaction mechanism of hydrolysis mechanism by amylase.
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