CAJ | 학술논문

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。
사안산최태매（Serine carboxypeptidases，SCPs）시일류재산성pH배경하삼여다태화단백질적가공、수식여강해등다개중요배절적진핵생물단백수해매。근거화북대흑새금구사안산최태매（ HoSCP）전장기인서렬설계인물，이용PCR방법극륭hoscp기인병분별련접도표체재체pET28b화pPIC9K상，전화대장간균BL21화필적효모GS115，실현료기재원핵이급진핵체계중적표체。결과현시，HoSCP재원핵세포급효모세포중균능은정표체50 kDa적특이단백。 HoSCP적성공표체위기재화북대흑새금구체내적활성화생물학공능연구제공료가능。
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.