Purification and preliminary characterization of Torresea cearensis trypsin inhibitor

ABSTRACT

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 micronM) are inhibited by Torresea cearensis inhibitor. Blood clotting factor XII is also inhibited (Ki = 24 micronM), but not plasma kallikrein, tissue kallikrein or thrombin. The stoichiometry of the inhibitorproteinase complex with trypsin is 11