Purification of RuBisCO from the Thermophilic Cyanobacterium Synechococcus sp. Strain a-1
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概要
- 論文の詳細を見る
Ribulose-1,5-bisphosphate carboxylase/oxygenase (RuBisCO), the key enzyme of the Calvin Benson cycle, has been purified from a thermophilic cyanobacterium, Synechococcus sp. strain a-1 and characterized. The enzyme is an L_8S_8-type hexadecamer with a molecular mass of 530 kDa. The enzyme was stable against heat treatment up to 70℃, which is the highest value among the RuBisCOs so far purified. The K_m value for ribulose bisphosphate on the carboxylase activity was substantially higher than those observed for RuBisCOs obtained from mesophilic autotrophs. The N-terminal amino acid sequence for the large subunit of the enzyme was highly similar to those of the other cyanobacteria despite the significant differences in heat stability.
- 社団法人日本生物工学会の論文
- 1992-05-25
著者
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IGARASHI Yasuo
Department of Biotechnology, The University of Tokyo
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Igarashi Y
Graduate School Of Agricultural And Life Sciences The University Of Tokyo
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Igarashi Yasuo
University Of Tokyo
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KODAMA Tohru
Department of Textile Science and Technology, Shinshu University
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Chung Seon
Laboratory Of Microbiology The Institute Of Physical And Chemical Research (riken)
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Chung S
Department Of Biotechnology University Of Tokyo
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Igarashi Y
Univ. Tokyo Tokyo Jpn
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Yaguchi Toshiaki
Department of Biotechnology, The University of Tokyo
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Chung Seong
Department of Biotechnology, The University of Tokyo
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Igarashi Yasuo
Department Of Agricultural Chemistry The University Of Tokyo
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Kokubo Tetsuro
Department Of Biotechnology The University Of Tokyo:(present Address)division Of Gene Function In An
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Chung Seong
Department Of Biotechnology University Of Tokyo
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YAGUCHI TOSHIAKI
Institute for Fundamental Research, Suntory Limited
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Yaguchi Toshiaki
Institute For Fundamental Research Suntory Limited
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Kodama Tohru
Department Of Agricultural Chemistry Faculty Of Agriculture The University Of Tokyo
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