The reaction products of myoglobin and simple phenolic compounds, with different configurations of hydroxyl groups, and p ‐quinone were characterized in terms of selected properties (electrophoretic, chromatographic and mass spectrometric) and by in vitro digestion. The o ‐, and p ‐hydroxyphenols, p ‐quinone and gallic acid showed high reactivity leading to structural changes in myoglobin. In comparison, ferulic acid and m ‐hydroxyphenol reacted to only a small extent, especially affecting tryptophan fluorescence of myoglobin. The enzymatic digestion (tryptic, a ‐chymotryptic, peptic and pancreatic), on the basis of in vitro experiments with derivatized myoglobin, was adversely influenced.
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Krôll et al. (2001) studied this question.
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