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Type: Artigo de periódico
Title: Trypsin inhibitor from Poecilanthe parviflora seeds: Purification, characterization, and activity against pest proteases
Author: Garcia, VA
Freire, MDM
Novello, JC
Marangoni, S
Macedo, MLR
Abstract: Plants synthesize a variety of molecules, including proteinaceous proteinase inhibitors, to defend themselves of being attacked by insects. In this work, a novel trypsin inhibitor (PPTI) was purified from the seeds of the native Brazilian tree Poecilanthe parviflora (Benth) (Papilioinodeae, Leguminosae) by gel filtration chromatography on a Sephadex G-100 followed by Superdex G75 chromatography (FPLC), Sepharose 4B-Trypsin column, and fractionated by reversed-phase HPLC on a C-18 column. SDS-PAGE showed that PPTI consisted of a single polypeptide chain with molecular mass of about 16 kDa. The dissociation constant of 1.0 x 10(-7) M was obtained with bovine trypsin. PPTI was stable over a wide range of temperature and pH and in the presence of DTT. The N-terminal sequence of the PPTI showed a high degree of homology with other Kunitz-type inhibitors. Trypsin-like activity in midguts of larval Diatraea saccharalis, Anagasta kuehniella, Spodoptera frugiperda, and Corcyra cephalonica were substantially inhibited by PPTI.
Subject: Kunitz inhibitor
pest protease
Poecilanthe parviflora
trypsin inhibitor
Country: EUA
Editor: Kluwer Academic/plenum Publ
Citation: Protein Journal. Kluwer Academic/plenum Publ, v. 23, n. 5, n. 343, n. 350, 2004.
Rights: fechado
Identifier DOI: 10.1023/B:JOPC.0000032654.67733.d5
Date Issue: 2004
Appears in Collections:Unicamp - Artigos e Outros Documentos

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