Identification of Bovine Skeletal Muscle Metmyoglobin Reductase as an NADH-Cytochrome b<sub>5</sub> Reductase

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  • ARIHARA Keizo
    School of Veterinary Medicine and Animal Sciences, Kitasato University
  • ITOH Makoto
    School of Veterinary Medicine and Animal Sciences, Kitasato University
  • KONDO Yo
    School of Veterinary Medicine and Animal Sciences, Kitasato University

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  • 牛骨格筋メトミオグロビン還元酵素のNADH-チトクロムb<sub>5</sub>還元酵素としての同定
  • ウシ コッカクキン メト ミオグロビン カンゲン コウソ ノ NADH チトク

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Abstract

Metmyoglobin reductase was purified from bovine skeletal muscle by procedures including affinity chromatography on a 5'-AMP-Sepharose 4B to an electrophoretically homogeneous protein. The enzyme had been purified over 20, 000 fold, and it has a pH optimum of 6.5. Molecular weight was estimated at 33, 000. Isoelectric pH was between 5.6-5.8. The enzyme reduced metmyoglobin in the presence of erythrocyte cytochrome b5. A Km for cytochrome b5 was 3.2×10-6M. These properties of the purified metmyoglobin reductase were similar to those of NADH-cytochrome b5 reductase purified from a bovine erythrocyte. Both enzymes were flavoproteins. Immunological studies have indicated that metmyoglobin reductase is indistinguishable from the erythrocyte enzyme. It was concluded, therefore, that bovine skeletal muscle metmyoglobin reductase was identical molecularly to erythrocyte NADH-cytochrome b5 reductase.

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