Purification of recombinant Pfu DNA polymerase using a new JK110 resin
Korean Journal of Chemical Engineering, ISSN: 0256-1115, Vol: 23, Issue: 4, Page: 607-609
2006
- 9Citations
- 34Captures
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Article Description
The purification of recombinant Pfu DNA polymerase expressed in Escherichia coli was studied. The lysed supernatant was heated to 75 °C to denature E. coli protein, followed by chromatography on JK110 and Sephadex G-75. The purified protein had comparable activity to the commercially obtained Pfu in both DNA polymerase and PCR amplification. The final product had a specific activity of 17,600 U/mg and 149,600 U of Pfu DNA polymerase was obtained from 500 ml culture. JK110 has worked well in our study and appears to be a new method of choice for purification of Pfu DNA polymerase.
Bibliographic Details
http://www.scopus.com/inward/record.url?partnerID=HzOxMe3b&scp=33751285233&origin=inward; http://dx.doi.org/10.1007/bf02706802; http://link.springer.com/10.1007/BF02706802; http://link.springer.com/content/pdf/10.1007/BF02706802; http://link.springer.com/content/pdf/10.1007/BF02706802.pdf; http://link.springer.com/article/10.1007/BF02706802/fulltext.html; http://www.springerlink.com/index/10.1007/BF02706802; http://www.springerlink.com/index/pdf/10.1007/BF02706802; https://dx.doi.org/10.1007/bf02706802; https://link.springer.com/article/10.1007/BF02706802
Springer Science and Business Media LLC
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