Abstract
A method is described for the preparation of native oxymyoglobin from bovine heart muscle. The aqueous extract is gel filtered on Sephadex G-50 to isolate myoglobin from hemoglobin. Native oxymyoglobin is then separated from metmyoglobin by DEAE-cellulose chromatography. There is a marked effect of temperature on the autoxidation of native oxymyoglobin to metmyoglobin, with Q 10 values approximating 5.3 over the pH range of 5–10. The activation energies over this pH range are shown to be almost constant, i.e., 26.5 kcal·mole −1. In contrast to the suggestions in earlier reports, the autoxidation rate of native oxymyoglobin estimated at physiological pH and temperature is quite high with t 1 2 ≤ 1.5 days under air saturation. This suggests the existence of an in vivo system(s) immediately reducing metmyoglobin formed to the ferrous state.
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