• Applied Biological Chemistry
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• v.37 no.5
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• pp.334-338
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• 1994

Streptococcal nuclease was completely purified by stepwise CM-Sepharose column chromatography from crude extracts isolated from Streptococcus sp. The active enzyme fraction was eluted with the buffer containing 0.2 M NaCl. The purified enzyme showed a homogeneity on SDS PAGE and had a molecular weight of 35,000 daltons. The optimum pH and temperature for the enzyme were 9.0 and $50^{\circ}C$, respectively.

• Journal of Microbiology and Biotechnology
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• v.4 no.4
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• pp.364-366
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• 1994

Molecular properties of streptococcal nuclease purified from Streptococcus sp. were examined. The purified enzyme was stable in the range of pH 7 to 10 and easily inactivated above $60^{\circ}C$. Atomic spectroscopy analysis indicated that the enzyme contains Ca, Mg, Zn. Circular dichroism study showed 25% $\alpha$ -helix, 15% $\beta$-sheet and 30% $\beta$-tums.