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Type: Artigo de periódico
Title: Purification And Characterization Of A New Trypsin Inhibitor From Dimorphandra Mollis Seeds.
Author: Mello, G C
Oliva, M L
Sumikawa, J T
Machado, O L
Marangoni, S
Novello, J C
Macedo, M L
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.
Subject: Animals
Plant Proteins
Substrate Specificity
Trypsin Inhibitors
Citation: Journal Of Protein Chemistry. v. 20, n. 8, p. 625-32, 2001-Nov.
Rights: fechado
Date Issue: 2001
Appears in Collections:Unicamp - Artigos e Outros Documentos

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