Please use this identifier to cite or link to this item: http://repositorio.unicamp.br/jspui/handle/REPOSIP/77043
Type: Artigo de periódico
Title: Trypsin inhibitor from Dimorphandra mollis seeds: purification and properties
Author: Macedo, MLR
de Matos, DGG
Machado, OLT
Marangoni, S
Novello, JC
Abstract: A trypsin inhibitor from Dimorphandra mollis seeds was isolated to apparent homogeneity by a combination of ammonium sulfate precipitation, gel filtration, ion-exchange and affinity chromatographic techniques. SDS-PAGE analysis gave an apparent molecular weight of 20 kDa, and isoelectric focusing analysis demonstrated the presence of three isoforms. The partial N-terminal amino acid sequence of the purified protein showed a high degree of homology with various members of the Kunitz family of inhibitors. This inhibitor, which inhibited trypsin activity with a K-i of 5.3 x 10(-10) M, is formed by a single polypeptide chain with an arginine residue in the reactive site. (C) 2000 Elsevier Science Ltd. All rights reserved.
Subject: Dimorphandra mollis
leguminosae
trypsin inhibitor
Kunitz inhibitor
N-terminal sequence
Country: Inglaterra
Editor: Pergamon-elsevier Science Ltd
Rights: fechado
Identifier DOI: 10.1016/S0031-9422(00)00155-2
Date Issue: 2000
Appears in Collections:Unicamp - Artigos e Outros Documentos

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