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- W2380147228 abstract "In this study,the DNA fragments of human neutrophil peptide 1(HNP-1) was synthesized according to the condon preference of E.coli and was linked with DsbA without signal peptide by means of SOE.Then,the product of SOE was inserted into vecter(pET11b) by the digesting of two restriction enzyme BamHⅠand NdeⅠ.After the recombinant plasmid(pET11b-DsbA-HNP-1) was transformed into E.coli JM109,the interested plasmid was extracted and transformed into E.coli BL21(DE3).The results indicated that the genetically engineered bacteria expressed a large quantity of intracellular and soluble DsbA-HNP-1 protein when it was inducted by IPTG,and the reconbinant HNP-1 fusion proteins possessed an antimicrobial activity to Bacillus pumilus after purified by Ni2+-Chelating chromatography and refoding in vitro." @default.
- W2380147228 created "2016-06-24" @default.
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- W2380147228 date "2008-01-01" @default.
- W2380147228 modified "2023-09-26" @default.
- W2380147228 title "Construction and soluble expression of fusion vector of human neutrophil peptide 1(HNP-1)" @default.
- W2380147228 hasPublicationYear "2008" @default.
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