| Literature DB >> 11890203 |
G C Mello1, M L Oliva, J T Sumikawa, O L Machado, S Marangoni, J C Novello, M L Macedo.
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.Entities:
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Year: 2001 PMID： 11890203 DOI： 10.1023/a:1013764118579
Source DB: PubMed Journal: J Protein Chem ISSN： 0277-8033