白蛋白修饰的人甲状旁腺激素的表达、纯化及活性鉴定  

Expression, Purification and Activity of A Fusion Protein PTH-HSA in Pichia Pastoris

作　　者：王一君 陈蕴 张莲芬 雷楗勇 陈其亮 李英 储敏 金坚 

机构地区：[1]江南大学医药学院细胞与分子药理实验室,江苏无锡214122

出　　处：《药物生物技术》2009年第1期8-13,共6页Pharmaceutical Biotechnology

基　　金：国家"863"计划项目(2006AA02Z153);上海市科委生物医药重大科技攻关项目(06DZ19020)

摘　　要：采用构建的含人甲状旁腺激素-血清白蛋白融合蛋白(PTH-HSA)的酵母工程菌Pichiapastoris进行表达条件研究,发酵上清中PTH-HSA表达量为171mg/L。发酵液经超滤浓缩。A fusion protein of Parathyroid hormone and human serum albumin （PTH-HSA） was ex- pressed and secreted into the fermentation broth with recombinant Pichia pastoris. The productivity of expressed PTH-HSA could reach 171mg/L. After being concentrated with ultrafiltration membrane, PTH-HSA was purified from fermentation broth by two different negative ion exchange chromatography and gel filtration chromatography in turn. It was concluded that a great deal of PTH-HSA with higher purity could be harvested by Pichia pastoris expression system and the established purification methods. Further studies show that PTH-HSA can significantly promote the effect on proliferation of osteoblasts cultured in vitro.

关 键 词：甲状旁腺激素 巴斯德毕赤酵母 融合蛋白 纯化 活性 成骨细胞 

分 类 号：R7[医药卫生—临床医学]