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  • Title: Purification and characterization of a new trypsin inhibitor from Dimorphandra mollis seeds.
    Author: Mello GC, Oliva ML, Sumikawa JT, Machado OL, Marangoni S, Novello JC, Macedo ML.
    Journal: J Protein Chem; 2001 Nov; 20(8):625-32. PubMed ID: 11890203.
    Abstract:
    A second trypsin inhibitor (DMTI-II) was purified from the seed of Dimorphandra mollis (Leguminosae-Mimosoideae) by ammonium sulfate precipitation (30-60%), gel filtration, and ion-exchange and affinity chromatography. A molecular weight of 23 kDa was estimated by gel filtration on a Superdex 75 column SDS-PAGE under reduced conditions showed that DMTI-II consisted of a single polypeptide chain, although isoelectric focusing revealed the presence of three isoforms. The dissociation constant of 1.7 x 10(-9) M with bovine trypsin indicated a high affinity between the inhibitor and this enzyme. The inhibitory activity was stable over a wide pH range and in the presence of DTT. The N-terminal sequence of DMTI-II showed a high degree of homology with other Kunitz-type inhibitors.
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