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  • Title: Trypsin inhibitor from Dimorphandra mollis seeds: purification and properties.
    Author: Macedo ML, de Matos DG, Machado OL, Marangoni S, Novello JC.
    Journal: Phytochemistry; 2000 Jul; 54(6):553-8. PubMed ID: 10963446.
    Abstract:
    A trypsin inhibitor from Dimorphandra mollis seeds was isolated to apparent homogeneity by a combination of ammonium sulfate precipitation, gel filtration, ion-exchange and affinity chromatographic techniques. SDS-PAGE analysis gave an apparent molecular weight of 20 kDa, and isoelectric focusing analysis demonstrated the presence of three isoforms. The partial N-terminal amino acid sequence of the purified protein showed a high degree of homology with various members of the Kunitz family of inhibitors. This inhibitor, which inhibited trypsin activity with a Ki of 5.3 x 10(-10) M, is formed by a single polypeptide chain with an arginine residue in the reactive site.
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