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Pancreatic trypsin is a serine protease that specifically cleaves peptide bonds C-terminal to a lysine or arginine residue.It is activated by a specific cleavage of the trypsinogen activation peptide following the sequence (Asp) 4-Lys.Several forms of recombinant protein precursors containing the bovine pancreatic trypsinogen were expressed as inclusion bodies in Escherichia coli T7 Express strain by fusion with polyhistidine and chitin binding domain tags.The tripartite precursors were solubilized under denaturing conditions and purified on single Ni-NTA resin at a yield of 30-40 mg/liter.