SUMMARYRates of autoxidation of beef and tuna oxymyoglobins have been determined at pH 5.9 with various buffer concentrations (0.1, 0.2, and 0.6M) and temperatures ranging from 0 to 40°C. The autoxidation is first‐order with respect to unoxidized myoglobin under all conditions used. The rates of oxidation of tuna oxymyoglobin were independent of buffer concentration, whereas those of beef myoglobin decreased with increasing buffer concentration. Tuna oxymyoglobin was oxidized more slowly than beef at 0 to 10°C at all buffer concentrations, and at higher temperatures and low buffer concentration; at high temperatures and high buffer concentration, tuna oxymyoglobin was oxidized more rapidly than beef. Oxidation of a crude preparation of beef oxymyoglobin was slower than that of purified myoglo
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