The intracellular proteinase enzymes of Penicillium griseofulvum and other fungi increase to levels several times higher than that in growing mycelium in the first few hours of nitrogen starvation, and remain at the higher level unless more assimilable nitrogen is supplied. The rise in proteinase does not take place in absence of oxygen or in the presence of p -fluorophenylalanine, and is not accompanied by net protein breakdown in the mycelium unless synthetic processes are inhibited by lack of oxygen or exogenous carbohydrate. The proteinase activity changes during the life cycle of the fungus, being absent in the spores, very low in the early stages of germination, and tending to rise steadily during growth. In some conditions the induction of sporulation is associated with a rise in proteinase, but there is no simple relation between the two processes. The results are considered to support the view that intracellular proteinase plays a part in protein turnover in the fungal cell.
Copyright (C) 1960, Society for Experimental Biology
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