文献类型：期刊文献

英文题名：High-level secretory expression, purification and characterization of Ailuropoda melanoleuca growth hormone in Pichia pastoris

作者：Xu, Qinggang[1,2];Wu, Xuechang[1];Hou, Rong[3];Liao, Mingjuan[1];Kim, Hyok Il[1];Shou, Jianxin[1,4];Bian, Hongwu[1];Han, Ning[1];Pan, Jianwei[1];Zhang, Zhihe[3];Zhu, Muyuan[1]

机构：[1]Zhejiang Univ, Coll Life Sci, Zijingang Campus,388 Yuhangtang Rd, Hangzhou 310058, Zhejiang, Peoples R China;[2]Jiangsu Univ, Inst Life Sci, Zhenjiang 212013, Peoples R China;[3]Joint Venture Minist Sci & Technol PR China & Sic, Dev Status State Key Lab, Key Lab Conservat Biol Endangered Wildlife, Chengdu 610081, Peoples R China;[4]Shaoxing Univ, Coll Life Sci, Shaoxing 312000, Peoples R China

年份：2008

卷号：60

期号：2

起止页码：182

外文期刊名：PROTEIN EXPRESSION AND PURIFICATION

收录：SCI-EXPANDED(收录号：WOS:000258016500014)、、WOS

语种：英文

外文关键词：AmGH; Ailuropoda melanoleuca; Pichia pastoris; expression; purification; characterization

外文摘要：Growth hormone is one of the most important hormones, which is involved in many reproductive processes of giant panda Ailuropoda melanoleuca. In this study, the mature peptide of A. melanoleuca growth hormone (AmGH) was successfully expressed and secreted in Pichia pastoris under the control of AOX1 promoter. The expression condition for AmGH in A pastoris, such as the expression time, pH value and methanol concentration in the BMMY were optimized and the AmGH expression level is about 100 mg/L using GS1 15 recombinant under optimized condition (96 h of 1.5% methanol induction). The secreted nascent AmGH were purified using ammonium sulfate fractionation. The mature AmGH protein exhibited a molecular mass of approximately 22 kDa on SDS-PAGE. This study would provide a new opportunity for large-scale expression and purification of AmGH, which might facilitate studies on the biological activity of AmGH. (c) 2008 Elsevier Inc. All rights reserved.