Temperature- and Detergent-Dependent Oligomeric Structures of Flavoprotein Monohydroxybenzoate Hydroxylases from Rhodococcus erythropolis

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概要

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• The results of analytical gel filtration chromatography experiments under various conditions showed each of three flavoprotein monohydroxybenzoate hydroxylases, p-hydroxybenzoate 3-hydroxylase, m-hydroxybenzoate 6-hydroxylase, and salicylate 5-hydroxylase, from the gram-positive Rhodococcus erythropolis strain S1 to by present in solution mainly as a tetramer at 4℃ and as a dimer at 30℃. In the presence of 1% Tween 80,the three flavoenzymes were each observed to be a monomer with activity about half that of the dimer.

• 社団法人日本生物工学会の論文
• 1996-08-25

著者

• NAKAJIMA Kenji

  Japan Atomic Energy Agency

• NAKAMURA Yoshihiro

  National Space Development Agency of Japan

• Suemori A

  National Inst. Biosci. And Human‐technol. (nibh) Ibaraki Jpn

• Suemori Akio

  National Institute Of Bioscience And Human-technology (nibh)

• KURANE Ryuichiro

  National Institute of Bioscience and Human-Technology (NIBH)

• NAKAJIMA KENJI

  National Institute of Bioscience and Human-Technology(NIBH)

• Nakajima K

  Japan Atomic Energy Agency

• Suemori A

  National Institute Of Bioscience And Human-technology (nibh)

• Nakajima K

  National Inst. Biosci. And Human‐technol. Ibaraki Jpn

• Nakamura Y

  Ajinomoto Co. Inc. Jpn

• Kurane R

  National Inst. Advanced Industrial Sci. And Technol. Tsukuba Jpn

• Nakajima Kenji

  National Institute Of Bioscience And Human-technology

• Kurane Ryuichiro

  National Institute Of Biosciecne And Human Technology Agency Of Industrial Science And Technology Ministry Of International Trade & Industry

• Nakamura Yoshihiro

  National Institute of Bioscience and Human-Technology (NIBH)

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