Expression and Purification of Recombinant 3C Proteinase of Coxsackievirus B3
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概要
- 論文の詳細を見る
We have cloned various lengths of coxsackievirus B3 cDNA encompassing the region encoding the 3C proteinase, which is essential to the viral replication cycle. Such viral cDNAs were fused in frame to the 5'terminal portion of the lacZ' gene carried on the vector pUCll8 to express mature 3C proteinase in Escherichia coli. In the E. coli cells containing pCXB108 or pCXB117,constructed for this study, a large amount of 23-kDa protein was synthesized in the presence of IPTG. This protein was purified and was shown to be intact 3C proteinase. These data suggest that 3C proteinase, expressed as a part of a fusion protein, was active in E. coli and released itself from the precursor fusion protein by autocatalytic cleavage.
- 社団法人日本農芸化学会の論文
- 1992-05-23
著者
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Komano T
Kyoto Univ. Kyoto Jpn
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Komano Tohru
Laboratory Of Biochemistry Department Of Agricultural Chemistry Kyoto University
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Komano Tohru
京都大学
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MIYASHITA Kinji
Central Research Laboratories, Maruishi Pharmaceutical Co., Ltd.
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UTSUMI Ryutaro
Laboratory of Biochemistry, Department of Agricultural Chemistry, Kinki University
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SATOH Nobukatsu
Central Research Laboratories, Maruishi Pharmaceutical Co., Ltd.
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Utsumi R
Department Of Bioscience And Biotechnology Graduate School Of Agriculture Kinki University
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Satoh Nobukatsu
Central Research Laboratories Maruishi Pharmaceutical Co. Ltd.
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KUSUMI Mikiko
Central Research Laboratories, Maruishi Pharmaceutical Co., Ltd.
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Miyashita Kinji
Central Research Laboratories Maruishi Pharmaceutical Co. Ltd.
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Komano T
Laboratory Of Cellular Biochemistry Division Of Applied Life Sciences Graduate School Of Agriculture
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Kusumi Mikiko
Central Research Laboratories Maruishi Pharmaceutical Co. Ltd.
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