Nuclease chromatographically purified after extraction from
Serratia marcescens was examined biochemically for some properties. The following results were obtained.
1) Twenty-three strains of
S. marcescens from human sources and of natural origin were examined for nuclease activity by the agar plate method. It was revealed that all the strains had nuclease activity to RNA and DNA.
2) DNA, RNA, and polynucleotides (RNase ‘core’) were degraded by the nuclease of
S. marcescens in the absence of inorganic phosphate. The optimal pH for hydrolysis of DNA and RNA was within the same pH range, and the stability of nuclease to heat was of the same grade for both substrates. In addition, from electrophoretic and immunological patterns, it was proved that nuclease might be homogeneous.
3) The nuclease activity of
S. marcescens was activated markedly in the presence of such cations as Mg
++, Mn
++, Fe
++, and Fe
+++, but was reduced by Hg
++, Zn
++, EDTA, citrate, and monoiodoacetic acid.
4) Digestion of yeast RNA and RNase ‘core’ with nuclease resulted in a rapid inactivation of their streptolysin S-producing activity.
5) From the results mentioned above, it was suggested that the extracellular nuclease of
S. marcescens might be regarded as a nonspecific phosphodiesterase on the basis of its activity.
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