Molecular characterization of a cDNA-derived phosphagen kinase from <i>Biomphalaria glabrata</i>, the intermediate host of <i>Schistosoma mansoni</i>
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- AGATSUMA Takeshi
- Department of Environmental Health Science, Kochi Medical School, Kochi University
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- FUKUNAGA Sae
- Department of Environmental Health Science, Kochi Medical School, Kochi University
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- JARILLA Blanca R.
- Department of Environmental Health Science, Kochi Medical School, Kochi University
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- NAGATAKI Mitsuru
- Department of Environmental Health Science, Kochi Medical School, Kochi University
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- TOKUHIRO Shinji
- Department of Environmental Health Science, Kochi Medical School, Kochi University
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- XIAO Jing-Ying
- Department of Environmental Health Science, Kochi Medical School, Kochi University
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- DEVI Kangjam R.
- Department of Environmental Health Science, Kochi Medical School, Kochi University
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- NOMURA Haruka
- Department of Environmental Health Science, Kochi Medical School, Kochi University
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- SHIMADA Masaaki
- Department of Eco-epidemiology, Institute of Tropical Medicine, Nagasaki University
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- UDA Kouji
- Laboratory of Biochemistry, Faculty of Science, Kochi University
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- SUZUKI Tomohiko
- Laboratory of Biochemistry, Faculty of Science, Kochi University
Bibliographic Information
- Other Title
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- マンソン住血吸虫症媒介中間宿主貝<i>Biomphalaria glabrata</i> cDNA由来フォスファーゲンキナーゼの分子生物学的研究
- Molecular characterization of a cDNA derived phosphagen kinase from Biomphalaria glabrata the intermediate host of Schistosoma mansoni
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Description
The present study contains the first description of phosphagen kinase (PK) from the intermediate snail host, Biomphalaria glabrata. We determined the cDNA sequence of PK from the snail B. glabrata, a vector of Schistosoma mansoni, and then cloned the cDNA into a pMAL plasmid and expressed it in Escherichia coli as a fusion protein with maltose-binding protein (MBP). The recombinant protein, consisting of 353 amino acids, has a calculated molecular mass of 39,376 Da and an estimated isoelectric point (pI) of 6.12. B. glabrata PK showed significant activity with the substrate L-arginine, indicating AK, and has the following kinetic constants determined for the forward reaction: KmArg=0.26 mM, KdArg=0.28 mM, kcat=20.3 s-1 and Vmax=30.4 μmol Pi/min/mg protein. Comparison of kcat/KmArg values with other AKs indicates that B. glabrata AK has a high catalytic efficiency (78.12 s-1 mM-1), although it exhibited weak synergism during substrate binding (KdArg/KmArg=1.08). In view of the significance of AK in temporal energy buffering, this enzyme may be a novel molluscicide target to control B. glabrata and consequently control the transmission of schistosomiasis.
Journal
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- Medical Entomology and Zoology
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Medical Entomology and Zoology 62 (1), 1-11, 2011
The Japan Society of Medical Entomology and Zoology
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Details 詳細情報について
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- CRID
- 1390001204940399360
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- NII Article ID
- 130004558985
- 10028089540
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- NII Book ID
- AN00021948
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- DOI
- 10.7601/mez.62.1
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- ISSN
- 21855609
- 04247086
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- NDL BIB ID
- 11068661
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- Text Lang
- en
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- Data Source
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- JaLC
- NDL
- Crossref
- CiNii Articles
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- Abstract License Flag
- Disallowed