ATP-inhibited ribonuclease of Bacillus subtilis I. Purification and general properties

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Abstract 1. 1. Ribonuclease (ribonucleate nucleotido-2′-transferase (cyclizing), EC 2.7.7.17) activity in the crude extract of Bacillus subtilis K was strongly inhibited by low concentrations of ATP. The inhibitory effect of ATP was thought to be common to all B. subtilis species. 2. 2. Ribonuclease in the crude extract was purified 2100-fold by means of DEAE-Sephadex A-50, Amberlite IRC-50 and Sephadex G-75 column chromatography, and the recovery was 26% efficient. 3. 3. The purified ribonuclease was shown to be almost homogeneous when tested by disc electrophoresis and was inhibited to an extent of 90% in the presence of 10 μM ATP. 4. 4. The ATP-inhibited ribonuclease showed optimum activity at pH 5.5–5.7, was stable between pH 7–8 and almost completely hydrolyzed yeast RNA. 5. 5. The degradation products were identified as Cyd-2′,3′-P, Urd-2′,3′-P, Ado-2′,3′-P and Guo-2′,3′-P.

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