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This remarkable experimental fact was discovered first on January 30, 1986 by the author and was recorded in a paragraph of the day of the author's working diary
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This remarkable experimental fact was discovered first on January 30, 1986 by the author and was recorded in a paragraph of the day of the author's working diary.
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(The 27th ESR Touronkai), Sendai Municipal Museum Hall, Miyagi, Japan, October 2729. (Abstracts pages 152154)
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M. Kohno, K. Mitsuta, Y. Mizuta, M. Hiramatsu, A. Mori, The 27th Annual Meeting of the Society of Electron Spin Resonance (The 27th ESR Touronkai), Sendai Municipal Museum Hall, Miyagi, Japan, October 2729, 1988, 29P02 (Abstracts pages 152154).
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(The 11th Jikikyoumei Igakukai), Matsuyama Postal Savings Hall, Ehime, Japan, May 1718, (Abstracts pages 9295)
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K. Mitsuta, Y. Mizuta, M. Kohno, The 11th Annual Meeting of Japan Society of Magnetic Resonance for Life Science (The 11th Jikikyoumei Igakukai), Matsuyama Postal Savings Hall, Ehime, Japan, May 1718, 1989, 1P11 (Abstracts pages 9295).
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The 11th Annual Meeting of Japan Society of Magnetic Resonance for Life Science
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(Jikikyoumei To Igaku 1), ed. by K. Ishizu, T. Yoshikawa, Nihon-Igakukan Co., Ltd., Tokyo
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77951177196
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For example, unpublished data about 3,3,5,5-tetramethyl-1- pyrroline N-oxide (M4PO). In the case of M4PO, the value of m1 seems to be larger than 1
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For example, unpublished data about 3,3,5,5-tetramethyl-1- pyrroline N-oxide (M4PO). In the case of M4PO, the value of m1 seems to be larger than 1.
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53
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77951202882
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6 M
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Milk xanthine oxidase is known to have an enzyme activity of more than 0.25 unit/mg protein and a molecular weight of ca. 300000. If 0.083 unit/mL XOD is converted into the molar concentration on the basis of these values, the result becomes ca. 1.1 × 106 M.
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54
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77951178406
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Based on eq 40 and the experimental conditions for 50% saturation (namely, kDMPO = 18M-1s-1, [DMPO] = 1.1 × 10-1 M, and [XOD] = 9.3 × 10-7 M) in our hypoxanthine-XOD system, the second-order rate constant kXOD for the reaction between XOD and O2-· is estimated to be roughly 2.1 × 106M-1 s-1 at pH 7.8. This value is 1.5 to 2.6 times that of 1.4 × 106 or 8.0 × 105M-1 s-1 estimated from our KO2system at pH 7.8. The cause of this difference seems to be the difference of the local pH of the reaction field in the early stage of the reaction between our two superoxide generating systems (Ref. 22)
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Based on eq 40 and the experimental conditions for 50% saturation (namely, kDMPO = 18M-1s-1, [DMPO] = 1.1 × 10-1 M, and [XOD] = 9.3 × 10-7 M) in our hypoxanthine-XOD system, the second-order rate constant kXOD for the reaction between XOD and O2-· is estimated to be roughly 2.1 × 106M-1 s-1 at pH 7.8. This value is 1.5 to 2.6 times that of 1.4 × 106 or 8.0 × 105M-1 s-1 estimated from our KO2system at pH 7.8. The cause of this difference seems to be the difference of the local pH of the reaction field in the early stage of the reaction between our two superoxide generating systems (Ref. 22).
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