Purification and preliminary characterization of Torresea cearensis trypsin inhibitor.

An inhibitor against serine proteinases was purified from Torresea cearensis by affinity chromatography on trypsin-Sepharose. The protein is a single polypeptide of molecular weight 13,600 after reduction and has a high content of cysteine residues. Both trypsin (Ki = 0.34 nM) and chymotrypsin (Ki = 0.15 microM) are inhibited by Torresea cearensis inhibitor. Blood clotting factor XII is also inhibited (Ki = 0.24 microM), but not plasma kallikrein, tissue kallikrein or thrombin. The stoichiometry of the inhibitor-proteinase complex with trypsin is 1:1.