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- W2367748249 abstract "Objective To study the expression of the extracellular fragment of P glycoprotein in the bacteria. Methods According to the P glycoprotein antigen analyses and mdr1 gene structure, a couple of primers were designed to amplify the extracellular DNA fragment of the protein with PCR. The product was inserted into pGEM T vector followed by sequencing. The sequencing verified vectors were cloned into pGEX 2T to get a highly expression recombinant vector pGEX Pgp. The recombinant was transferred into E. coli DH5α, and its expression, identification and purification were studied. Results The highest level of recombinant expression was achieved at 4 h after IPTG induction. SDS PAGE analysis indicated that the expressed protein was about 30×10 3. Conclusion The target gene fragment expression at high level is established for the preparation of its antibody and biospanning of its specific peptide by using random phage library, founding a basis for the targeting treatment of multidrug resistance." @default.
- W2367748249 created "2016-06-24" @default.
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- W2367748249 date "2003-01-01" @default.
- W2367748249 modified "2023-09-25" @default.
- W2367748249 title "Expression of fused P-glycoprotein in E. coli DH5α" @default.
- W2367748249 hasPublicationYear "2003" @default.
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