Abstract
1. 1. Chicken serum strongly inhibited a fungal protease from Aspergillus melleus. This inhibitor was purified by ammonium sulfate fractionation, column chromatography on DEAE-Toyopearl and Blue-Toyopearl and HPLC gel filtration. 2. 2. During purification, the chicken inhibitor was found to be strongly adsorbed in Cibacron Blue. 3. 3. The purified inhibitor gave a single protein band with a mol. wt of about 60,000 on SDS-polyacrylamide gel electrophoresis. 4. 4. This inhibitor showed high heat, pH and urea stability and represented strong inhibitory activity against fungal proteases and subtilisin. 5. 5. Two-dimensional electrophoresis revealed eight molecular species with slightly different charges and similar mol. wts. 6. 6. Neuraminidase treatment suggested that the microheterogeneity of the inhibitor molecule is due to the variation in sialic acid content.
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