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 …