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KMID : 0903519940370050334
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Journal of the Korean Society of Agricultural Chemistry and Biotechnology
1994 Volume.37 No. 5 p.334 ~ p.338
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Puriification of Streptococcal nuclease from Streptococcus sp .
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Song Kyung-Bin
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Abstract
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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℃, respectively.
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