Cloning,expression, and antitumor activity of recombinant protein of curcin |
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Authors: | M J Luo W X Liu X Y Yang Y Xu F Yan P Huang F Chen |
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Institution: | (1) College of Life and Science, Sichuan University 24, South Section 1, Yihuan Road, Chengdu, Sichuan, 610041, China;(2) Chengdu Institute for Family Planning, Chengdu, 610031, China |
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Abstract: | Curcin, a protein isolated from the seeds of Jatropha curcas can be used as a cell-killing agent. To elaborate the purification methods and investigate the antitumor activity of the
recombinant protein, the fragment encoding the mature protein of curcin was inserted into E. coli strain M15 and the recombinant strain was induced to express by the optimum inducer (0.5 mM isopropyl-β-D-thiogalactopyranoside).
The recombinant protein was expressed in the form of the inclusion body and was purified by Ni-NTA affinity chromatography.
The protein of interest was incubated with the tumor cells at various concentrations for different time. It was shown that
the target protein could inhibit the growth of NCL-H446, SGC-7901, and S180 at a very low concentration.
Published in Russian in Fiziologiya Rastenii, 2007, Vol. 54, No. 2, pp. 229–234.
The text was submitted by the authors in English. |
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Keywords: | Jatropha curcas Esherichia coli curcin expression purification recombinant protein antitumor activity |
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