2013 Fiscal Year Final Research Report
Development of anti-Trypanosoma drug based on structural and functional analysis of novel L-amino acid dehydrogenase
| Project/Area Number |
24780105
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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 |
Applied biochemistry
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| Research Institution | Tokai University |
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Principal Investigator |
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| Project Period (FY) |
2012-04-01 – 2014-03-31
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| Keywords | 酵素化学 / L-スレオニン酸脱水素酵素 / NAD / トリパノソーマ |
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| Research Abstract |
L-Threonine dehydrogenase (ThrDH) gene from the pathogenic parasite Trypanosoma brucei was amplified using the overlapping primers, and ligated with the expression vector pCold TF. Escherichia coli was then transformed with the vector and induced by adding 1.0 mM IPTG to the medium. The gene was overexpressed in E. coli, and its product was purified and characterized. SDS-PAGE showed the subunit molecular mass of T. brucei ThrDH to be about 81 kDa, which was consistent with the molecular weight calculated from the amino acid sequence. The slightly NAD-dependent ThrDH activity was determined.
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