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RISS 인기검색어
- 검색키워드
- 주제어 : Deinococcus radiophilus (검색결과 4 건)
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- 기관 내 무료
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Production of Superoxide Dismutase by Deinococcus radiophilus
Yun, Young-Sun,Lee, Young-Nam Korean Society for Biochemistry and Molecular Biol 2003 Journal of biochemistry and molecular biology Vol.36 No.3
The production of superoxide dismutase (SOD) varied in Deinococcus radiophilus, the UV resistant bacterium, depending upon different phases of growth, UV irradiation, and superoxide treatment. A gradual increase in total SOD activity occurred up to the stationary phases. The electrophoretic resolution of the SOD in cell extracts of D. radiophilus at each growth phase revealed the occurrence of MnSOD throughout the growth phases. The SOD profiles of D. radiophilus at the exponential phase received oxidative stress by the potassium superoxide treatment or UV irradiation also revealed the occurrence of a single SOD. However, these treatments caused an increase in SOD activity. The data strongly suggest that D. radiophilus has only one species of SOD as a constitutive enzyme, which seems to be a membrane-associated protein.
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Production of Superoxide Dismutase by Deinococcus radiophilus
( Young Sun Yun ),( Young Nam Lee ) 생화학분자생물학회 2003 BMB Reports Vol.36 No.3
The production of superoxide dismutase (SOD) varied in Deinococcus rdiophilus, the UV resistant bacterium, depending upon different phases of growth, UV irradiation, and superoxide treatment. A gradual increase in total SOD activity occurred up to the stationary phases. The electrophoretic resolution of the SOD in cell extracts of D. radiophilus at each growth phase revealed the occurrence of MnSOD throughout the growth phases. The SOD profiles of D, rdiophilus at the exponential phase received oxidative stress by the potassium superoxide treatment of UV irrdadiation also revealed the occurrence of a single SOD. However, these treatments caused an increase in SOD activity. The data strongly suggest that D.radiophilus has only one species of SOD as a constitutive enzyme, which seems to be a membrane-associated protein.
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Purification and Characterization of Catalase-2 from Deinococcus radiophilus
Lee,Young Nam,Oh,Kyung-A The Korea Science and Technology Center 1998 BMB Reports Vol.31 No.2
A bifunctional catalase-peroxidase, designated catalase-2, of a UV resistant Deinococcus radiophilus was purified to electrophoretic homogeneity by both chromatograpic and electrophoretic methods. Its molecular weight was 310kDa and composed of a tetramer of 80 kDa subunits. The catalase-2 exerted its optical activity at 30℃ and around pH 9. Its Km value for H₂O₂was about 10 mM. It showed the typical ferric heme spectrum with maximum absorption at 403 nm which shifted to 419 nm in the presence of cyanide. The ratio of A403/A280 was 0.48. Fifty percent inhibition of the enzyme activity was observed at 4.6×10-6 7.7×10-6, and 3.0×10?/M of NaCN, NaN₃, and NH₂OH, respectively. The enzyme was thermostable and not sensitive to 3-amino-1,2,4-triazole. Treatment of the enzyme with ethanol-chloroform caused a partial loss(30%) of its activity. The catalase-2 was distinct form the Deinococcal bifunctional catalase-3 in a number of properties, particularly in its molecular structure and substrate affinity.
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Purification and Characterization of Catalase-2 from Deinococcus radiophilus
Oh, Kyung-A,Lee, Young-Nam Korean Society for Biochemistry and Molecular Biol 1998 Journal of biochemistry and molecular biology Vol.31 No.2
A bifunctional catalase-peroxidase, designated catalase-2, of a UV resistant Deinococcus radiophilus was purified to electrophoretic homogeneity by both chromatographic and electrophoretic methods. Its molecular weight was 310 kDa and composed of a tetramer of 80 kDa subunits. The catalase-2 exerted its optimal activity at $30^{\circ}C$ and around pH 9. Its $K_m$ value for $H_{2}0_{2} $ was about 10 mM. It showed the typical ferric heme spectrum with maximum absorption at 403 nm which shifted to 419 nm in the presence of cyanide. The ratio of A40i' A2S0 was 0.48. Fifty percent inhibition of the enzyme activity was observed at $4.6{\times}10^{-6}$, $7.7{\times}10^{-6}$, and $3.0{\times}10^{-6}$ M of NaCN, $NaN_3$, and $NH_{2}OH$, respectively. The enzyme was thermostable and not sensitive to 3-amino-1,2,4-triazole. Treatment of the enzyme with ethanol-chloroform caused a partial loss (30%) of its activity. The catalase-2 was distinct from the Deinococcal bifunctional catalase-3 in a number of properties, particularly in its molecular structure and substrate affinity.
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