Improvement of Purification Method for Brucella Outer Membrane Protein 16

The high level expression of recombinant proteins in E.coli often leads to the formation of inclusion bodies that contain most of the expressed protein.That affects the protein purification efficiency and purity.In order to improve the protein purification efficiency and purity,we used improved methods to purify the Brucellaouter membrane protein(Omp16);The fragment Omp16 was amplified by PCR,and then connected to the PET32-a vector,transformed into E.coli BL21,induced its expression,recombinant proteins was purified through HISnickel protein purification column.The results showed that the Brucellaouter membrane protein Omp16 in soluble protein increased,the efficiency of protein outputs and purity was improved.This study made the purification procedure,and may be helpful for efficient purification of recombinant proteins.