Cloning and expression of the gene encoding Acacia confusa trypsin inhibitor that is active without post-translational proteolysis
Journal
Gene
Journal Volume
127
Journal Issue
2
Pages
215-219
Date Issued
1993
Author(s)
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.
Type
journal article