Isolation of a ribonuclease from fruiting bodies of the wild mushroom Termitomyces globulus.

A ribonuclease, with a molecular mass of 13 kDa and a ubiquitin-like N-terminal sequence, has been isolated from fruiting bodies of the mushroom Termitomyces globulus. The ribonuclease demonstrated ribonucleolytic activity toward poly A, poly C, poly G and poly U, with the activity toward poly A and poly C being much higher than that toward poly G and poly U. The ribonuclease was unadsorbed on DEAE-cellulose but adsorbed on Affi-gel blue gel and CM-Sepharose. The enzyme required a temperature of 70 degrees C for expression of maximal activity. However, the enzyme expressed nearly the same optimal activity over a wide pH range of 5.0-8.0.