Purification and Properties of Adenosine 5'-Triphosphate Sulfurylase from the Thermophilic Bacterium Bacillus stearothermophilus
スポンサーリンク
概要
- 論文の詳細を見る
ATP sulfurylase, which catalyzes the first step on the sulfate activation, was purified to apparent homogeneity from Bacillus stearothermophilus, with ammonium sulfate fractionation and successive column chromatography. The enzyme had an apparent molecular mass of 100 kDa, consisting of two equal-sized-44 kDa subunits. The optimum pH was about 8.5-8.7. Divalent cations such as Mn^<2+>, Mg^<2+>, and Co^<2+> were required for its activity. Apparent K_m values for ATP and SO_4^<2-> were 0.045 mM and 0.2 mM, respectively. The enzyme can use deoxyadenosine 5'-triphosphate as a substrate. The enzyme was thermostable and did not show significant loss of activity for 15 min of incubation up to 70℃, suggesting a practical use for a continuous reaction.
- 社団法人日本農芸化学会の論文
- 1996-10-23
著者
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NAKAJIMA Hiroshi
Department of Earth and Space Science, Osaka University
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Onda Masaaki
Department of Biology, Faculty of Science, Osaka University
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IWATA Ken
Department of Orthopedic Surgery, Faculty of Medicine, Kagawa University
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Nakajima Hiroshi
Department Of Biochemistry Central Research Institute Maruha Corporation
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Onda Masaaki
Department Of Biochemistry Unitika Research And Development Center
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Iwata Ken
Department Of Orthopaedic Surgery Kagawa University Faculty Of Medicine
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MORIM0TO Akemi
Department of Biochemistry, Unitika Research and Development Center
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SIMOIDE Ayako
Department of Biochemistry, Unitika Research and Development Center
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Simoide Ayako
Department Of Biochemistry Unitika Research And Development Center
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Morim0to Akemi
Department Of Biochemistry Unitika Research And Development Center
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Iwata Ken
Department Of Biochemistry Unitika Research And Development Center
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NAKAJIMA Hiroshi
Department of Allergy and Clinical Immunology, Chiba University Hospital
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