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|Type:||Artigo de periódico|
|Title:||Purification and characterization of a new trypsin inhibitor from Dimorphandra mollis seeds|
|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.|
|Editor:||Kluwer Academic/plenum Publ|
|Citation:||Journal Of Protein Chemistry. Kluwer Academic/plenum Publ, v. 20, n. 8, n. 625, n. 632, 2001.|
|Appears in Collections:||Unicamp - Artigos e Outros Documentos|
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