The properties of crude phosphodiesterase forming 5'-mononucleotide of Pellicularia H-11 were investigated on its metal requirement, pH response for activity and so on. The dialyzate of crude PDase against distilled water became partly inactive, but was recovered with Zn⁺⁺, Mn⁺⁺ and Mg⁺⁺, whereas completely inactivated dialyzate against EDTA was restored specifically with only Zn⁺⁺
The optimum pH of PDase activity was 5.0 and that of ribonuclease 4.0. The crude PDase was partially purified by acetone fractionation and Amberlite IRC-50 (XE-64) or CM-cellulose column chromatography. Two PDase and a RNase activities were recognized.
Pellicularia PDase was found to be of new type according to its Zn⁺⁺ dependency and non-activity towards bis-p-nitrophenyl phosphate.

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