摘要
丝氨酸羧肽酶(Serine carboxypeptidases,SCPs)是一类在酸性pH环境下参与多肽和蛋白质的加工、修饰与降解等多个重要环节的真核生物蛋白水解酶。根据华北大黑鳃金龟丝氨酸羧肽酶(HoSCP)全长基因序列设计引物,利用PCR方法克隆hoscp基因并分别连接到表达载体pET28b和pPIC9K上,转化大肠杆菌BL21和毕赤酵母GS115,实现了其在原核以及真核体系中的表达。结果显示,HoSCP在原核细胞及酵母细胞中均能稳定表达50 kDa的特异蛋白。HoSCP的成功表达为其在华北大黑鳃金龟体内的活性和生物学功能研究提供了可能。
Serine carboxypeptidases （ SCPs ） are a class of protease enzyme that play essential roles in a wide range of biological processes which are the modification and degradation of peptides and proteins .We report ,in this study ,the hoscp gene of Holotrichia oblita was amplified by PCR method and cloned into the expression vector pET 28b and pPIC9K,respectively .The following recombinant vector was transformed into Escherichia coli BL21 and Pichia pastoris GS115,respectively .The results showed that HoSCP was stably expressed as a 50 kDa recombinant protein in E.coli and P.pastoris.It is useful for the further study of activity and biological function of HoSCP in H.oblita.
出处
《华北农学报》
CSCD
北大核心
2013年第5期44-47,共4页
Acta Agriculturae Boreali-Sinica
基金
国家重点基础研究发展规划("973"计划)项目(2009CB118902)
国家自然科学基金项目(30971910)
国家现代农业产业技术体系项目
