Molecular cloning, expression and identification of recombinant hyaluronan synthase from Pasteurella multocida

VernacularTitle:重组巴氏杆菌透明质酸合成酶的克隆、表达及活性鉴定
Author: Chen PENG ; Hao GE ; Shuying HE ; Xiangdong GAO
Publication Type:Journal Article
Keywords: rPmHAS; expression; purification; identification
From: Journal of China Pharmaceutical University 2009;40(6):549-552
CountryChina
Language:Chinese
Abstract: Aim: To set a suitable route for efficient expression and purification of recombinant hyaluronan syn-thase from Pasteurella multocida (rPmH AS). Methods: Coding sequences were cloned and expressed in Esche-richia coli strain of BL-21( DE3). Then rPmHAS was purified through a simple Ni-affinity chromatography and identified by hyaluronic acid binding protein ( HABP) based ELISA assay. Results: High yield expression of functional rPmHAS exceeding the highest production reported hitherto was achieved, and the purity of rPmHAS was as high as 90%. Conclusion: In this study, an optimized system of the expression, purification and identifica-tion route for large scale preparation of rPmHAS was established, which will be helpful for accelerating further study of PmHAS and facilitating fine researches on peculiar hyaluronic acid with special properties.