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• W2034665708 abstract "Bovine serum albumin (BSA) was used as a probe for the oxidation of proteins by hypervalent myoglobin species in solutions with pH from 5.3 to 7.7. The reaction between perferrylmyoglobin, *MbFe(IV)=O, and BSA was studied by activating metmyoglobin with equimolar amounts of hydrogen peroxide in the presence of BSA. A minor pH dependence was observed as judged from the formation of BSA-centered radicals, which were monitored at room temperature by electron spin resonance spectroscopy, and the formation of dityrosine. The reaction between ferrylmyoglobin, MbFe(IV)=O, and BSA was pH-dependent. BSA-centered radicals and dityrosine were formed in low levels at neutral pH and increased at low pH to the same levels as observed in the reaction of *MbFe(IV)=O with BSA. The present results demonstrate that protein-centered radicals can be formed from the non-radical MbFe(IV)=O under mildly acidic conditions, and this should be taken into account when considering oxidation in cellular compartments of low pH and in meat-related products." @default.
• W2034665708 created "2016-06-24" @default.
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• W2034665708 date "2003-08-01" @default.
• W2034665708 modified "2023-10-11" @default.
• W2034665708 title "The effect of pH on the oxidation of bovine serum albumin by hypervalent myoglobin species" @default.
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• W2034665708 doi "https://doi.org/10.1016/s0003-9861(03)00317-5" @default.
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