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  • Title: Purification and preliminary characterization of Torresea cearensis trypsin inhibitor.
    Author: Tanaka AS, Sampaio MU, Sampaio CA, Oliva ML.
    Journal: Braz J Med Biol Res; 1989; 22(9):1069-71. PubMed ID: 2636004.
    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 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.
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