Mammalian tyrosinase; effect of ions on enzyme action.
نویسنده
چکیده
Recent investigations of mammalian tyrosinase have shown the relationship of some chemical and physical factors to tyrosinase activity (1,2,3). Whereas the effect of temperature, pH, lyophilization, oxidation-reduction potentials, and concentrations of enzyme and substrate have been studied, the effect of different ions and ionic concentration on tyrosinase activity has not been described. Hence, it was decided t,o study the influence of various electrolytes on mammalian tyrosinase. It was hoped that some information would be obtained regarding the mechanism of tyrosinase action as well as the means by which copper is bound to this enzyme. The inhibition of melanin formation by some metal ions was studied in particular.
منابع مشابه
In vitro and in silico studies of the inhibitory effects of some novel kojic acid derivatives on tyrosinase enzyme
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Copper has been reported to be an essential part of the enzyme tyrosinase prepared from various plant and insect sources (l-8). In the case of potato tyrosinase, Kubowitz (1, 2) found that the enzyme could be inhibited by reagents which combine with copper, e.g. diethyldithiocarbamate, salicylaldoxime, and carbon monoxide. He demonstrated that treatment of the enzyme with cyanide followed by di...
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ورودعنوان ژورنال:
- Archives of biochemistry and biophysics
دوره 36 2 شماره
صفحات -
تاریخ انتشار 1952