Please use this identifier to cite or link to this item: http://repositorio.unicamp.br/jspui/handle/REPOSIP/348895
Type: Artigo
Title: Purification and characterization of a trypsin inhibitor from Plathymenia foliolosa seeds
Author: Ramos, Vanessa Da Silveira
Silva, Gilvania De Souza
Machado Freire, Maria Das Gracas
Tavares Machado, Olga Lima
Postali Parra, Jose Roberto
Rodrigues Macedo, Maria Ligia
Abstract: A novel trypsin inhibitor (PFTI) was isolated from Plathymenia foliolosa (Benth.) seeds by gel filtration chromatography on a Sephadex G-100, DEAE-Sepharose, and trypsin-Sepharose columns. By SDS-PAGE, PFTI yielded a single band with a M-r of 19 kDa. PFTI inhibited bovine trypsin and bovine chymotrypsin with equilibrium dissociation constants (K-i) of 4 x 10(-8) and 1.4 x 10(-6) M, respectively. PFTI retained more than 50% of activity at up to 50 degrees C for 30 min, but there were 80 and 100% losses of activity at 60 and 70 degrees C, respectively. DTT affected the activity or stability of PFTI. The N-terminal amino acid sequence of PFTI showed a high degree of homology with various members of the Kunitz family of inhibitors. Anagasta kuehniella is found worldwide; this insect attacks stored grains and products of rice, oat, rye, corn, and wheat. The velvet bean caterpillar (Anticarsia gemmatalis) is considered the main defoliator pest of soybean in Brazil. Diatraea saccharalis, the sugar cane borer, is the major pest of sugar cane crops, and its caterpillar-feeding behavior, inside the stems, hampers control. PFTI showed significant inhibitory activity against trypsin-like proteases present in the larval midguts on A. kuehniella and D. saccharalis and could suppress the growth of larvae
Subject: Inibidores da tripsina
Country: Estados Unidos
Editor: American Chemical Society
Rights: Fechado
Identifier DOI: 10.1021/jf802778b
Address: https://pubs.acs.org/doi/10.1021/jf802778b
Date Issue: 2008
Appears in Collections:IB - Artigos e Outros Documentos

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