Purification and Characterization of Cysteine Proteinase from a Baculovirus Gene
スポンサーリンク
概要
- 論文の詳細を見る
To analyze the degradation of product proteins at the late stage of virus infection in the baculovirus expression system, a cysteine proteinase was purified from hemolymph of Bombyx mori infected with wild-type B. mori nuclear polyhedorosis virus (BmNPV). The purified cysteine proteinase preparation had two protein bands (major 35-kDa active protein and 28-kDa inactive protein) on SDS-PAGE. Based on the N-terminal amino acid sequences of them, it was found that both proteins originated in the cysteine proteinase gene of BmNPV. The purified cysteine proteinase had an optimum pH at 4.0, and also had activities at neutral pHs. When recombinant luciferase was used as a natural substrate, it was degraded rapidly by the cysteine proteinase at the physiological pH of hemolymph. These results suggest that the cysteine proteinase from a BmNPV gene participates in the degradation of foreign protein expressed by the baculovirus system.
- 社団法人日本農芸化学会の論文
- 1997-09-23
著者
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Suzuki Tomomi
School Of Agriculture Bioscience Center Nagoya University
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ODA Kohei
Department of Applied Biology, Kyoto Institute of Technology
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Sugiyama Tatsuo
Riken Plant Science Center
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Takahashi S
Akita Res. Inst. Food And Brewing Akita
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Suzuki T
Division Of Marine Life Sciences Grauate School Of Fisheries Science Hokkaido University
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TAKAHASHI Saori
Department of Bioengineering, Akita Research Institute of Food and Brewing (ARIF)
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Oda Kohei
Department Of Applied Biology Faculty Of Textile Science Kyoto Institute Of Technology
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Oda Kohei
Department Of Agricultural Chemistry College Of Agriculture University Of Osaka Prefecture
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Ogawa Katsuaki
Katakura Industries Co. Ltd.
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USHIYAMA Souko
Department of Applied Biology, Faculty of Textile Science, Kyoto Institute of Technology
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SUZUKI Takeo
Katakura Industries Co., Ltd.
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Suzuki Takahito
Biological Laboratory Faculty Of Science Nara Women's University
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Takahashi Saori
Department Of Applied Biology Faculty Of Textile Science Kyoto Institute Of Technology
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