Cloning and Expression of the Sarcosine Oxidase Gene from Bacillus sp. NS-129 in Escherichia coli(Biological Chemistry)
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概要
- 論文の詳細を見る
The gene coding for a thermostable sarcosine oxidase (EC 1.5.3.1) was isolated from Bacillus sp. NS-129. The primary structure of sarcosine oxidase deduced from the nucleotide sequence was a protein composed of 387 amino acids with molecular weight 42,955. When the sarcosine oxidase was overproduced to about 35% of soluble protein in E. coli under the control of a lac promoter, the sarcosine oxidase activity of the crude extract was increased 3-fold by the addition of FAD. This indicates that most of the enzyme is accumulated in an inactive form, a flavinless aporotein, in the cell.
- 社団法人日本農芸化学会の論文
- 1991-05-23
著者
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Koyama Y
Laboratory Of Cellular Biochemistry Graduate School Of Nutritional And Environmental Sciences Univer
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Nakano Eiichi
Research And Development Division Kikkoman Corporation
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Nakano Eiichi
Department Of Cardiovascular Surgery Research Institute Of Angiocardiology Kyushu University Faculty
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Koyama Yasuji
Research And Development Division Kikkoman Corporation
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Koyama Yu
Cellular Biochemistry School Of Food And Nutritional Sciences University Of Shizuoka
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Koyama Yu
Laboratory Of Cellular Biochemistry Graduate School Of Nutritional And Environmental Sciences Univer
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Yamamoto-otake Hideko
Research And Development Division Kikkoman Corporation
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Nakano E
Kikkoman Corp. Chiba
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SUZUKI MASARU
Research and Development Division, Kikkoman Corporation
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Suzuki M
National Research Inst. Fisheries Science Ministry Of Agriculture Forestry And Fisheries Tokyo Jpn
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Suzuki Masaru
Research & Development Division Kikkoman Corporation
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