Abstract
Crystalline prepns. of ribonuclease invariably possessed proteolytic activity, which varied in amt. in different prepns. The pH zones of proteolytic and ribonuclease activities were somewhat d ifferent. Between pH 4 and 4.5 only the ribonuclease activity, though far from its opt., was demonstrable. By heating at. pH 7 - 7.5 under specified conditions, the proteolytic activity was greatly reduced or destroyed, leaving between 30-80% of the original ribonuclease activity. Ribonuclease was attacked by pepsin, chymotrypsin, and the proteolytic enzyme of crystalline prepns. of ribonuclease.