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- W2354709729 abstract "In order to study the optimal expression and purification condition of the GLP-1 derived polypeptide,by PCR technology synthetizing the gene of the GLP-1 derived polypeptide with preference codon of E.coli with the plasmid containing human wild-type GLP-1 gene.Expressed fusion proteins were purified and desalted with Ni-NTA column and C18 Sep-Pak column,respectively.After chemical cleavaged by formic acid hydroformicant,the hydrolysis products were purified with Ni-NTA column and HPLC.The target peptide was identified by mass spectrum.Experiment results showed in E.coli BL21 the optimal expression condition as follow:inducing temperature is 37℃,inducing time is 6h,and the concentration of the IPTG is 0.6mmol/L.The optimal chromatographic condition of getting HPLC as follow:mobile phase A(10% CNCH3∶90% H2O,0.1%TFA),mobile phase B(100% CNCH3,0.1% TFA),flow rate is 1ml/min,30 min of the linear gradient elution,B phase reaches 70% and the detection wave length is 280nm.The molecular mass of the GLP-1 derived polypeptide is 5.492 kDa,through mass spectrum identification.The yield of GLP-1 derived polypeptide prepared with the optimal expression and purification condition may reach 11.6mg/L fermentation product and its purity is equal or greater than 98%." @default.
- W2354709729 created "2016-06-24" @default.
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- W2354709729 date "2009-01-01" @default.
- W2354709729 modified "2023-09-26" @default.
- W2354709729 title "Expression of Gene Recombinant GLP-1 Derived Polypeptide and Its Purification and Identification" @default.
- W2354709729 hasPublicationYear "2009" @default.
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