Abstract
A chymotrypsin inhibitor of the Kazal-type has been isolated from duck pancreas, by affinity chromatography on immobilized chymotrypsin, gel filtration on Bio-Gel P-10 and reverse phase (RP)-HPLC. It inhibits bovine chymotrypsin Aα with an association constant ( K a) of 2.06×10 7 M −1. The complete amino acid sequence was determined after digestion of pyridylethylated inhibitor with Staphylococcus aureus V8 protease and chemical cleavage with CNBr. Duck pancreatic chymotrypsin inhibitor (DPCI) was found to be a single polypeptide chain composed of 65 amino acid residues, corresponding to a molecular mass of 7191 Da.
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