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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 ionexchange 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 ́ 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. ©2002 Plenum Publishing Corporation.|
|Appears in Collections:||Unicamp - Artigos e Outros Documentos|
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