Abstract
IT is well known that tyrosinase becomes inactivated when it oxidizes phenol or pyrocatechol but is much more stable towards substituted phenols and catechols, such as 4-5-dimethyl catechol1. We wish to report evidence which seems to support the view that this inactivation is due to the formation of a compound between the enzyme protein and the product of oxidation.
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References
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WOOD, B., INGRAHAM, L. Labelled Tyrosinase from Labelled Substrate. Nature 205, 291–292 (1965). https://doi.org/10.1038/205291a0
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DOI: https://doi.org/10.1038/205291a0
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