Purification and characterization of a new trypsin inhibitor from Dimorphandra mollis seeds

  • Mello G
  • Oliva M
  • Sumikawa J
 et al. 
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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.

Author-supplied keywords

  • Dimorphandra mollis
  • Kunitz family
  • Mimosoideae
  • N-terminal sequence
  • Trypsin inhibitor

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