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Cloning and expression of the gene encoding Acacia confusa trypsin inhibitor that is active without post-translational proteolysis.

作者信息

Hung C H, Lee M C, Lin M T, Lin J Y

机构信息

Institute of Biochemistry, College of Medicine, National Taiwan University, Taipei, ROC.

出版信息

Gene. 1993 May 30;127(2):215-9. doi: 10.1016/0378-1119(93)90722-f.

DOI:10.1016/0378-1119(93)90722-f
PMID:8500764
Abstract

A recombinant plasmid containing the coding regions for Acacia confusa trypsin inhibitor (ACTI) has been constructed and expressed in Escherichia coli cells, as a fusion protein between ACTI and glutathione S-transferase (GST). The GST-fusion was produced as a soluble protein which did not require denaturing agents such as urea to solubilize it. The recombinant ACTI (reACTI) was obtained by treating the GST-fusion protein with thrombin. Both the reACTI and fusion protein have a strong inhibitory effect on trypsin activity without post-translational proteolysis.

摘要

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