A protease inhibitor produced by Penicillium cyclopium on solid sultures of wheat bran was purified by means of column chromatography on Duolite A-2 and DEAE-cellulose. acetone precipitation and lyophilization. The purified inhibitor obtained as a white, floccose and hygroscopic substance was monodisperse by ultracentrifugal analysis. It was found to be an acidic macro-molecule of a molecular weight of about 5000. The chemical analyses rejected the possibility of the presence of amino acids, peptides, sugars, amino sugars, or uronic acids in the inhibitor molecule.
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Shimada et al. (1969) studied this question.
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