Show simple item record

dc.contributor.authorWicaksono, Imam Adi
dc.contributor.authorLestari, Tresna
dc.contributor.authorUlfa, Evi Umayah
dc.contributor.authorRiyani, Catur
dc.contributor.authorElfahmi
dc.date.accessioned2015-10-30T04:22:25Z
dc.date.available2015-10-30T04:22:25Z
dc.date.issued2015-10-30
dc.identifier.citation[1] Duffy PE, Mutabingwa TK, Artemisinin combination therapies, Lancet, 367, 2037–2039, 2006. [2] Hale, V., Keasling, JD., Renninger, N and Diagana, N.N, Microbially Derived Artemisinin: A Biotechnology Solution to the Global Problem of Access to Affordable Antimalarial Drugs, Am. J. Trop. Med. Hyg., 77(Suppl 6), 198–202, 2007. [3] Julsing, M. K., Pouderoyen G. V., Veen J. V., Woerdenbag H. J., Bioconversion and combinatorial biosynthesis of selected terpenoids and lignans, Thesis, Department of Pharmaceutical Biology of The University of Groningen, Netherlands, 4, 47-56, 2006. [4] Li Y, Huang H, Wu YL, Qinghaosu (artemisinin)—a fantastic antimalarial drug from a traditional Chinese medicine, In: Liang XT, Fang WS (eds) Medicinal Chemistry of Bioactive Natural Products, Wiley, New York, pp 183–256, 2006. [5] Mutabingwa TK. Artemisinin-based combination therapies (ACTs): best hope for malaria treatment but inaccessible to the needy! Acta Trop. 95:305–315. doi: 10.1016/j.actatropica.2005.06.009. [6] Rathore, D., McCutchan, T.F., Sullivan, M., and Kumar, S., Antimalarial drugs: current status and new developments. Expert Opin. Investig. Drugs, 14, 871–883. doi:10.1517/13543784.14.7. 871. PMID:16022576, 2005. [7] White NJ, Qinghaosu (artemisinin): the price of success, Science, 320, 330–334, 2008. [8] Wladyka, B., Puzia, K., and Dubin, A., Efficient Coexpression of a Recombinant Staphopain A and Its Inhibitor Staphostatin A, Biochem. J., 385, 181-187, 2005.in_ID
dc.identifier.issn9-772476-969006
dc.identifier.urihttp://hdl.handle.net/11617/6191
dc.description.abstractCYP71AV1 and ADS are two enzymes involved in artemisinin biosynthesis. In this research, sub-cloning of cyp71av1 and ads in pETDUET1 (pETDUET1_cyp/ads) has been done. The result of transformation has been confirmed by migration, restriction and sequencing analysis. Overproduction of CYP71AV1 and ADS was done at temperature 37 °C using 0,5 mM IPTG induction. The protein produced mostly formed as inclusion bodies, therefore the optimization of overproduction condition is still needed.in_ID
dc.language.isoenin_ID
dc.publisherUniversitas Muhammadiyah Surakartain_ID
dc.subjectCYP71AVin_ID
dc.subjectADSin_ID
dc.subjectpETDUET1in_ID
dc.subjectSub-cloningin_ID
dc.titleSub-Cloning of ads Gene Into pETDUET1_cyp For Co-Expression in Escherichia coliin_ID
dc.typeArticlein_ID


Files in this item

Thumbnail

This item appears in the following Collection(s)

  • ICB-PHARMA II
    Current Breakthrough in Pharmacy Materials and Analyses

Show simple item record