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  • Title: Purification and characterization of two Kunitz family subtilisin inhibitors from seeds of Canavalia lineata.
    Author: Terada S, Fujimura S, Katayama H, Nagasawa M, Kimoto E.
    Journal: J Biochem; 1994 Mar; 115(3):392-6. PubMed ID: 8056748.
    Abstract:
    Two subtilisin inhibitors (CLSI-II and -III) were purified from seeds of Canavalia lineata by extraction with water, ammonium sulfate precipitation, and chromatographies on DEAE-Toyopearl and hydroxyapatite. The two inhibitors have the same molecular weight of about 22,000, and quite similar amino acid compositions. They contain five half-cystine residues and tend to dimerize through an intermolecular disulfide bridge due to the presence of a single cysteine residue. CLSI-III only inhibited subtilisin-type serine proteases, while CLSI-II showed a wider inhibitory specificity. Though the two inhibitors have almost identical thermal labilities, CLSI-II is more stable as to extreme pH than CLSI-III. They are considered to be Kunitz type inhibitors on the basis of several properties.
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