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dc.contributor.authorLuo, M. J.-
dc.contributor.authorLiu, W. X.-
dc.contributor.authorYang, X. Y.-
dc.contributor.authorXu, Y.-
dc.contributor.authorYan, F.-
dc.contributor.authorHuang, P.-
dc.contributor.authorChen, F.-
dc.date.accessioned2011-11-26T05:33:38Z-
dc.date.available2011-11-26T05:33:38Z-
dc.date.issued2007-
dc.identifier.citationVol. 54, No. 2, pp. 202–206.en_US
dc.identifier.issn1021-4437-
dc.identifier.urihttp://dspace.unimap.edu.my/123456789/16352-
dc.description.abstractCurcin, 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.en_US
dc.language.isoenen_US
dc.publisherRussian in Fiziologiya Rasteniien_US
dc.relation.ispartofseriesRussian Journal of Plant Physiologyen_US
dc.subjectJatropha curcasen_US
dc.subjectEsherichia colien_US
dc.subjectCurcinen_US
dc.subjectExpressionen_US
dc.subjectPurificationen_US
dc.subjectRecombinant proteinen_US
dc.subjectAntitumor activityen_US
dc.titleCloning, Expression, and Antitumor Activity of Recombinant Protein of Curcinen_US
dc.typeArticleen_US
dc.identifier.doi10.1134/S1021443707020070-
dc.contributor.urlchengfang@scu.edu.cnen_US
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