سال انتشار: ۱۳۸۴

محل انتشار: چهارمین همایش ملی بیوتکنولوژی ایران

تعداد صفحات: ۲

نویسنده(ها):

Mansour Abachi – Biotechnology department, Pasteur institute, Tehran
Ali Moradi – Biotechnology department, Pasteur institute, Tehran
Maryam Omidi – Biotechnology department, Pasteur institute, Tehran
Atousa Aliahmadi – Biotechnology department, Pasteur institute, Tehran

چکیده:

There are many methods for the production of recombinant human insulin in microorganisms. One typical scheme for preparing human insulin utilizes proinsulin that is produced in E.coli cytoplasm as an inclusion body of a fusion protein. In this study, BL21 (DE3) was used as the expression host. The expression vector was pET32-a which contains thioredoxin tag as a fusion partner. The result showed high ability of thioredoxin in reduction of disulphide bridge in proinsulin when it was expressed as inclusion body.