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http://repositorio.unicamp.br/jspui/handle/REPOSIP/77044
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 Leguminosae 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 |
Files in This Item:
File | Description | Size | Format | |
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WOS000223042600006.pdf | 133.9 kB | Adobe PDF | View/Open |
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