Detection of a proteinase inhibitor in Aspergillus nidulans.
The activity of proteinases in mycelial extracts of Aspergillus nidulans increased during storage. The rate of activation increased with temperature. Three separate proteinase activities, differing in their electrophoretic mobilities on polyacrylamide gels, were readily detected at pH 6.5. Inhibitory activity, effective against all three proteinase activities, was also detected in fractions prepared from fresh mycelial extracts. The inhibitory factor(s) were heat-stable and non-dialysable. The inhibitory activity was lost during storage of mycelial extracts. It is proposed that the inhibitory factor(s) are digested by the proteinases during storage.
D001233:Aspergillus nidulans / Q000201:enzymology*; D004591:Electrophoresis, Polyacrylamide Gel; D004789:Enzyme Activation; D007527:Isoenzymes / Q000378:metabolism; D010447:Peptide Hydrolases / Q000378:metabolism; D011309:Preservation, Biological; D011480:Protease Inhibitors / Q000378:metabolism*; D013696:Temperature
D007527:Isoenzymes; D011480:Protease Inhibitors; D010447:Peptide Hydrolases