Abstract
The presence of two distinct molecular structures for tyrosinase in fungi is confirmed. The enzyme from Agaricus bisporus is acidic and comprises two dissimilar subunits which aggregate to form a tetramer. This tetramer constitutes the majority both in the resting and functional states. In Neurospora crassa, tyrosinase is slightly basic and contains only one subunit, similar in size to the larger subunit of the Agaricus enzyme. In the resting state Neurospora tyrosinase is distributed among a number of forms, from the monomer to the tetramer. In this case it was possible to show that a species smaller than the tetramer, probably the monomer, was fully active.
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