SUMMARY: The decline in activity of extracellular laccase of which occurs during fruit body development was shown to be due to both enzyme inactivation and proteolysis. Extracts of high activity, from cultures during mycelial growth, and of low activity, from cultures during fruiting, remained unchanged on prolonged incubation and did not cross-activate or inhibit on mixing. No activity changes occurred after dialysis, gel filtration or ultrafiltration of both forms. Molecular weights, pH optima, substrate specificities and immunological properties of the two forms were identical. Differences were found in the electrophoretic profiles of the two forms of enzyme. Loss of enzyme activity was shown to be greater than loss of enzyme protein by separate immunological and electrophoretic methods.


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