Purification and Properties of Gentisate 1,2-Dioxygenase from Rhodococcus erythropolis S-1
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概要
- 論文の詳細を見る
Gentisate 1,2-dioxygenase, which participates in salicylate and m-hydroxybenzoate metabolism, was purified from cell-free extracts of Rhodococcus erythropolis S-1, a Gram-positive bacterium. The purified enzyme gave a single band on native PAGE and SDS-PAGE. The molecular mass of the enzyme was estimated to be 328kDa. The structure of the enzyme appears to be an octamer of identical subunits. The enzyme from this bacterium was similar in general enzymatic properties to a gentisate 1,2-dioxygenase from a Gram-negative bacterium except for molecular mass and structure.
- 社団法人日本農芸化学会の論文
- 1993-10-23
著者
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Suemori A
National Inst. Biosci. And Human‐technol. (nibh) Ibaraki Jpn
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Suemori Akio
National Institute Of Bioscience And Human-technology (nibh)
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KURANE Ryuichiro
National Institute of Bioscience and Human-Technology (NIBH)
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TOMIZUKA NOBORU
Department of Food Science and Technology, Faculty of Bioindustry, Tokyo University of Agriculture
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Tomizuka Noboru
National Institute of Bioscience and Human-Technology (NIBH)
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Tomizuka Noboru
National Institute Of Bioscience And Human-technology
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Kurane R
National Inst. Advanced Industrial Sci. And Technol. Tsukuba Jpn
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Kurane Ryuichiro
National Institute Of Biosciecne And Human Technology Agency Of Industrial Science And Technology Ministry Of International Trade & Industry
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