[in Japanese]

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A bacteriolytic enzyme obtained from the culture filtrate of Aspergillus melleus was purified by disc electrophoresis and examined for its properties enzymologically and immunologically.
The enzyme was a DFP-sensitive alkaline protease, having residues of either tryptophane, tyrosine, or histidine. Neither metal chelating agents nor thiol poisons inhibited the activity of this proteolytic enzyme.
From experiments concerning the enzymatic inhibition using either bacterial cells or pure casein as the substrates, it was suggested that the bacteriolytic activity of this enzyme was based on its nature to hydrolyze the peptide bonds of the peptidoglycan, a major component of the bacterial cell wall.
In the rabbit sera immunized with this enzyme, there were detected neutralizing and precipitating antibodies which reacted with homologous antigen as well as commercial protease originated from Aspergillus oryzae. However, the antibodies made no response with purified trypsin, reflecting the immunological difference between trypsin and above mentioned fungal proteases.

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A septum-rich fraction was prepared from Triehophyton mentagrophytes, and the ultrastructural investigation of septa was carried out by shadowing and thin section electron microscopy before and after enzymatic and/or alkaline treatments. Tri-lamellar structure, consisting of an electron lucid middle layer and two outer electron dense layers, was observed by thin section electron microscopy. By shadowing electron microscopy, the surface ultrastructure of septa exhibited a randomly orientated microfibrillar network structure, which may correspond to the electron dense outer layers of the septum observed in thin section preparations. However, shadowed septa after papain digestion revealed a spiral arrangement of microfibrils consisting of rodlet-like units, which disappeared during chitinase treatment. This spiral structure may therefore be composed primarily of chitin. It was suggested that this spirally arranged microfibrils may correspond to the electron lucid middle layer observed in thin section preparations.

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[in Japanese]

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