INTRACELLULAR RIBONUCLEASE OF BACILLUS SUBTILIS - SPECIFIC INHIBITION BY ATP AND DATP

Ribonuclease activity in the crude extract of Bacillus subtilis was strongly inhibited by low concentration of ATP. Ribonuclease in the extract was purified by 2100 times to almost homogeneous state as tested by disc electrophoresis. The purified enzyme hydrolyzed RNA to Ado-2′:3′-P, Guo-2′:3′-P, Cyd-2′:3′-P, Urd-2′:3′-P and was specifically inhibited by ATP and dATP. Ki values for ATP and dATP were 0.12 and 0.21 μM respectively. The mode of inhibition of ATP was competitive. © 1969.