P40蛋白在大肠杆菌内的表达及初步纯化

摘要

To obtain purified P40 protein for the further study on its function.Sequence coding for protein P40 was amplified from whole p40 gene by PCR method and cloned into pGEX|4tl vector for expression.Expressed protein induced by IPTG was then purified with glutathione agrose by means of affinity chromatography.Results showed that the coding sequence of a new gene we cloned previously could be expressed in E.coli with the form of fusion with GST and the fusion protein existed in inclusion bodies of the bacteria.