Purification, and activity of Human rhinovirus 3C protease fused with N-terminal GST-tag and C-terminal His-tag (GST-HRV3C-His) expressed in Escherichia coli

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Tác giả: Duong Vuong Le, Thi Tuong Vy Le, Duc Hoang Nguyen, Thi Phuong Trang Phan

Ngôn ngữ: Vie

Ký hiệu phân loại:

Thông tin xuất bản: Tạp chí Khoa học Trường Đại học Sư phạm Thành phố Hồ Chí Minh , 2019

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Bộ sưu tập: Metadata

ID: 418538

The Human rhinovirus 3C protease (HRV3C) is one of the most effective enzymes for removing fusion tag in purification process. This protease is often produced as fusion form GST-HRV3C but there is no study about the fusion form GST-HRV3C-His. In this study, researchers conducted the purification GST-HRV3C-His expressed in E. coli, checked the activity and investigated its application. GST-HRV3C-His could be purified using His-tag column with 86.6% purity and GST column with 96.87%. The specific activity of GST-HRV3C-His was demonstrated to be about 4500 U/mg and its application in the purification of another proteins carrying HRV3C-specific recognition sequence, LEVLFQ¯GP based on His-tag or GST-tag was also proved in this study.
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