Analysis of oxidation-reduction process of hemoproteins in steer muscle by nitrite.

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  • TACHIYASHIKI Kaoru
    Department of Living and Health Sciences, Joetsu University of Education
  • UESUGI Kuniko
    Department of Living and Health Sciences, Joetsu University of Education
  • IMAIZUMI Kazuhiko
    Department of Living and Health Sciences, Joetsu University of Education

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Other Title
  • 亜硝酸イオンによる牛筋組織中のヘムタンパク質の酸化還元反応過程の解析
  • アショウサン イオン ニ ヨル ウシ キン ソシキチュウ ノ ヘム タンパクシ

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Abstract

The reaction processes of oxidation and reduction of hemoproteins in steer muscle by nitrite (NO2-) were kinetically studied. Oxyhemoglobin (HbO2) was used to compare with muscle hemoproteins in the oxidation process. Oxidation of muscle hemoproteins and HbO2 by NO2- proceeded according to the apparent first order kinetics and the sigmoidal mode, respectively. The addition of H2O2 or catalase clearly modified the oxidation of HbO2 but not of muscle hemoprotein. Muscle hemes and HbO2 differed significantly in the mode of oxidation of hemoprotein by NO2-. The reduction rate of muscle met-hemes increased with the decrease of [NO2-] / [heme] at pH 6.0 and 7.4 and at 5°C. The reduction rate of muscle met-hemes was about 20% higher at pH 7.4 than that at pH 6.0. When [NO2-] / [heme] was 1 at pH 7.4, about 16 days were essential to the complete reduction of musclemet-hemes. The absorption spectrum of muscle hemes after complete reduction was similar to that of HbNO or MbNO.

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