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
Nelson, J. M., and Dawson, C. R., Adv. Enz., 4, 99 (1944).
Frieden, E., and Ottesen, M., Biochim. Biophys. Acta, 34, 248 (1959).
Waley, S. G., and Watson, J., Biochem. J., 55, 328 (1953).
Raper, H. S., J. Chem. Soc., 125 (1938).
Mason, H. S., J. Biol. Chem., 172, 83 (1948).
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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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